Molecular Motors in Myelination and Their Misregulation in Disease.
Demyelinating diseases
Dynein
Kinesins
Multiple sclerosis
Myelination
Myosins
Journal
Molecular neurobiology
ISSN: 1559-1182
Titre abrégé: Mol Neurobiol
Pays: United States
ID NLM: 8900963
Informations de publication
Date de publication:
31 Oct 2024
31 Oct 2024
Historique:
received:
28
09
2023
accepted:
21
10
2024
medline:
31
10
2024
pubmed:
31
10
2024
entrez:
31
10
2024
Statut:
aheadofprint
Résumé
Molecular motors are cellular components involved in the intracellular transport of organelles and materials to ensure cell homeostasis. This is particularly relevant in neurons, where the synaptic components synthesized in the soma need to travel over long distances to their destination. They can walk on microtubules (kinesins and dyneins) or actin filaments (myosins), the major components of cell cytoskeleton. While kinesins mostly perform the anterograde transport of intracellular components toward the plus ends of microtubules located distally in cell processes, cytoplasmic dyneins allow the retrograde flux of intracellular cargo toward the minus ends of microtubules located at the cell soma. Axon myelination represents a major aspect of neuronal maturation and is essential for neuronal function, as it speeds up the transmission of electrical signals. Increasing evidence supports a role for molecular motors in the homeostatic control of myelination. This role includes the trafficking of myelin components along the processes of myelinating cells and local regulation of pathways that ensure axon wrapping. Dysfunctional control of the intracellular transport machinery has therefore been linked to several brain pathologies, including demyelinating diseases. These disorders include a broad spectrum of conditions characterized by pathological demyelination of axons within the nervous system, ultimately leading to axonal degeneration and neuronal death, with multiple sclerosis representing the most prevalent and studied condition. This review highlights the involvement of molecular motors in the homeostatic control of myelination. It also discusses studies that have yielded insights into the dysfunctional activity of molecular motors in the pathophysiology of multiple sclerosis.
Identifiants
pubmed: 39477877
doi: 10.1007/s12035-024-04576-9
pii: 10.1007/s12035-024-04576-9
doi:
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Cooperativa de Ensino Superior Politécnico e Universitário
ID : Mddemy-GI2-CESPU-2022
Organisme : Fundação para a Ciência e a Tecnologia
ID : UIDP/04378/2020
Organisme : Fundação para a Ciência e a Tecnologia
ID : UIDB/04378/2020
Organisme : Fundação para a Ciência e a Tecnologia
ID : DL57/2016/CP1355/CT0007
Organisme : Secretaria Regional do Mar, Ciência e Tecnologia
ID : SFRH/BD/144877/2019
Informations de copyright
© 2024. The Author(s).
Références
Guedes-Dias P, Holzbaur ELF (2019) Axonal transport: driving synaptic function. Science 366:eaaw9997. https://doi.org/10.1126/science.aaw9997
doi: 10.1126/science.aaw9997
pubmed: 31601744
pmcid: 6996143
Cianfrocco MA, DeSantis ME, Leschziner AE, Reck-Peterson SL (2015) Mechanism and regulation of cytoplasmic dynein. Annu Rev Cell Dev Biol 31:83–108. https://doi.org/10.1146/annurev-cellbio-100814-125438
doi: 10.1146/annurev-cellbio-100814-125438
pubmed: 26436706
pmcid: 4644480
Lu W, Gelfand VI (2017) Moonlighting motors: kinesin, dynein, and cell polarity. Trends Cell Biol 27:505–514. https://doi.org/10.1016/j.tcb.2017.02.005
doi: 10.1016/j.tcb.2017.02.005
pubmed: 28284467
pmcid: 5476484
Cason SE, Holzbaur ELF (2022) Selective motor activation in organelle transport along axons. Nat Rev Mol Cell Biol 23:699–714. https://doi.org/10.1038/s41580-022-00491-w
doi: 10.1038/s41580-022-00491-w
pubmed: 35637414
Guillaud L, El-Agamy SE, Otsuki M, Terenzio M (2020) Anterograde axonal transport in neuronal homeostasis and disease. Front Mol Neurosci 13:556175. https://doi.org/10.3389/fnmol.2020.556175
doi: 10.3389/fnmol.2020.556175
pubmed: 33071754
pmcid: 7531239
Lu W, Gelfand VI (2022) Go with the flow – bulk transport by molecular motors. J Cell Sci 136. https://doi.org/10.1242/jcs.260300
Bercury KK, Macklin WB (2015) Dynamics and mechanisms of CNS myelination. Dev Cell 32:447–458. https://doi.org/10.1016/j.devcel.2015.01.016
doi: 10.1016/j.devcel.2015.01.016
pubmed: 25710531
pmcid: 6715306
Shelestak J, Irfan M, DeSilva TM (2022) Remyelinating strategies: what can be learned from normal brain development. Curr Opin Pharmacol 67:102290. https://doi.org/10.1016/j.coph.2022.102290
doi: 10.1016/j.coph.2022.102290
pubmed: 36195009
Fletcher JL, Makowiecki K, Cullen CL, Young KM (2021) Oligodendrogenesis and myelination regulate cortical development, plasticity and circuit function. Semin Cell Dev Biol 118:14–23. https://doi.org/10.1016/j.semcdb.2021.03.017
doi: 10.1016/j.semcdb.2021.03.017
pubmed: 33863642
Lyons DA, Naylor SG, Scholze A, Talbot WS (2009) Kif1b is essential for mRNA localization in oligodendrocytes and development of myelinated axons. Nat Genet 41:854–858. https://doi.org/10.1038/ng.376
doi: 10.1038/ng.376
pubmed: 19503091
pmcid: 2702462
Bolis A, Coviello S, Visigalli I, Taveggia C, Bachi A, Chishti AH, Hanada T, Quattrini A, Previtali SC, Biffi A, Bolino A (2009) Dlg1, Sec8, and Mtmr2 regulate membrane homeostasis in Schwann cell myelination. J Neurosci 29:8858–8870. https://doi.org/10.1523/jneurosci.1423-09.2009
doi: 10.1523/jneurosci.1423-09.2009
pubmed: 19587293
pmcid: 6664895
Langworthy MM, Appel B (2012) Schwann cell myelination requires Dynein function. Neural Dev 7:37. https://doi.org/10.1186/1749-8104-7-37
doi: 10.1186/1749-8104-7-37
pubmed: 23167977
pmcid: 3520773
Wang H, Tewari A, Einheber S, Salzer JL, Melendez-Vasquez CV (2008) Myosin II has distinct functions in PNS and CNS myelin sheath formation. J Cell Biol 182:1171–1184. https://doi.org/10.1083/jcb.200802091
doi: 10.1083/jcb.200802091
pubmed: 18794332
pmcid: 2542477
Love S (2006) Demyelinating diseases. J Clin Pathol 59:1151–1159. https://doi.org/10.1136/jcp.2005.031195
doi: 10.1136/jcp.2005.031195
pubmed: 17071802
pmcid: 1860500
Javed A, Arnason BGW (2009) Demyelinating diseases. In: Squire LR (ed) Encyclopedia of neuroscience. Academic Press, Oxford, pp 415–422
doi: 10.1016/B978-008045046-9.00575-1
Barkhof F, Koeller KK (2020) Demyelinating diseases of the CNS (brain and spine). In: Hodler J, Kubik-Huch RA, von Schulthess GK (eds) Diseases of the brain, head and neck, Spine 2020–2023: Diagnostic Imaging. Springer International Publishing, Cham, pp 165–176
doi: 10.1007/978-3-030-38490-6_13
Popescu BFG, Lucchinetti CF (2012) Pathology of demyelinating diseases. Annu Rev Pathol 7:185–217. https://doi.org/10.1146/annurev-pathol-011811-132443
doi: 10.1146/annurev-pathol-011811-132443
pubmed: 22313379
Kamil K, Yazid MD, Idrus RBH, Das S, Kumar J (2019) Peripheral demyelinating diseases: from biology to translational medicine. Front Neurol 10:87. https://doi.org/10.3389/fneur.2019.00087
doi: 10.3389/fneur.2019.00087
pubmed: 30941082
pmcid: 6433847
Beijer D, Sisto A, Van Lent J, Baets J, Timmerman V (2019) Defects in axonal transport in inherited neuropathies. J Neuromuscul Dis 6:401–419. https://doi.org/10.3233/JND-190427
doi: 10.3233/JND-190427
pubmed: 31561383
pmcid: 6918914
Sweeney HL, Holzbaur ELF (2018) Motor proteins. Cold Spring Harb Perspect Biol 10:a021931. https://doi.org/10.1101/cshperspect.a021931
doi: 10.1101/cshperspect.a021931
pubmed: 29716949
pmcid: 5932582
McIntosh BB, Ostap EM (2016) Myosin-I molecular motors at a glance. J Cell Sci 129:2689–2695. https://doi.org/10.1242/jcs.186403
doi: 10.1242/jcs.186403
pubmed: 27401928
pmcid: 4958297
Quintanilla MA, Hammer JA, Beach JR (2023) Non-muscle myosin 2 at a glance. J Cell Sci 136:jcs260890. https://doi.org/10.1242/jcs.260890
doi: 10.1242/jcs.260890
pubmed: 36917212
pmcid: 10411949
Olenick MA, Holzbaur ELF (2019) Dynein activators and adaptors at a glance. J Cell Sci 132:jcs227132. https://doi.org/10.1242/jcs.227132
doi: 10.1242/jcs.227132
pubmed: 30877148
pmcid: 6451413
Rao L, Gennerich A (2024) Structure and function of dynein’s non-catalytic subunits. Cells 13:300. https://doi.org/10.3390/cells13040330
doi: 10.3390/cells13040330
Braschi B, Omran H, Witman GB, Pazour GJ, Pfister KK, Bruford EA, King SM (2022) Consensus nomenclature for dyneins and associated assembly factors. J Cell Biol 221:e202109014. https://doi.org/10.1083/jcb.202109014
doi: 10.1083/jcb.202109014
pubmed: 35006274
pmcid: 8754002
Vuolo L, Stevenson NL, Mukhopadhyay AG, Roberts AJ, Stephens DJ (2020) Cytoplasmic dynein-2 at a glance. J Cell Sci 133:jcs240614. https://doi.org/10.1242/jcs.240614
doi: 10.1242/jcs.240614
pubmed: 32229580
Hirokawa N, Noda Y, Tanaka Y, Niwa S (2009) Kinesin superfamily motor proteins and intracellular transport. Nat Rev Mol Cell Biol 10:682–696. https://doi.org/10.1038/nrm2774
doi: 10.1038/nrm2774
pubmed: 19773780
Endow SA, Kull FJ, Liu H (2010) Kinesins at a glance. J Cell Sci 123:3420–3424. https://doi.org/10.1242/jcs.064113
doi: 10.1242/jcs.064113
pubmed: 20930137
pmcid: 2951464
Hartman MA, Spudich JA (2012) The myosin superfamily at a glance. J Cell Sci 125:1627–1632. https://doi.org/10.1242/jcs.094300
doi: 10.1242/jcs.094300
pubmed: 22566666
pmcid: 3346823
Foth BJ, Goedecke MC, Soldati D (2006) New insights into myosin evolution and classification. Proc Natl Acad Sci U S A 103:3681–3686. https://doi.org/10.1073/pnas.0506307103
doi: 10.1073/pnas.0506307103
pubmed: 16505385
pmcid: 1533776
Wells AL, Lin AW, Chen LQ, Safer D, Cain SM, Hasson T, Carragher BO, Milligan RA, Sweeney HL (1999) Myosin VI is an actin-based motor that moves backwards. Nature 401:505–508. https://doi.org/10.1038/46835
doi: 10.1038/46835
pubmed: 10519557
Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P (2002) Molecular biology of the cell. Garland Science, New York
Wong S, Weisman LS (2021) Roles and regulation of myosin V interaction with cargo. Adv Biol Regul 79:100787. https://doi.org/10.1016/j.jbior.2021.100787
doi: 10.1016/j.jbior.2021.100787
pubmed: 33541831
pmcid: 7920922
Li S, Mecca A, Kim J, Caprara GA, Wagner EL, Du T-T, Petrov L, Xu W, Cui R, Rebustini IT, Kachar B, Peng AW, Shin J-B (2020) Myosin-VIIa is expressed in multiple isoforms and essential for tensioning the hair cell mechanotransduction complex. Nat Commun 11:2066. https://doi.org/10.1038/s41467-020-15936-z
doi: 10.1038/s41467-020-15936-z
pubmed: 32350269
pmcid: 7190839
Vale RD, Funatsu T, Pierce DW, Romberg L, Harada Y, Yanagida T (1996) Direct observation of single kinesin molecules moving along microtubules. Nature 380:451–453. https://doi.org/10.1038/380451a0
doi: 10.1038/380451a0
pubmed: 8602245
pmcid: 2852185
Kim AJ, Endow SA (2000) A kinesin family tree. J Cell Sci 113:3681–3682. https://doi.org/10.1242/jcs.113.21.3681
doi: 10.1242/jcs.113.21.3681
pubmed: 11034894
Lawrence CJ, Dawe RK, Christie KR, Cleveland DW, Dawson SC, Endow SA, Goldstein LSB, Goodson HV, Hirokawa N, Howard J, Malmberg RL, McIntosh JR, Miki H, Mitchison TJ, Okada Y, Reddy ASN, Saxton WM, Schliwa M, Scholey JM, Vale RD, Walczak CE, Wordeman L (2004) A standardized kinesin nomenclature. J Cell Biol 167:19–22. https://doi.org/10.1083/jcb.200408113
doi: 10.1083/jcb.200408113
pubmed: 15479732
pmcid: 2041940
Walczak CE, Gayek S, Ohi R (2013) Microtubule-depolymerizing kinesins. Annu Rev Cell Dev Biol 29:417–441. https://doi.org/10.1146/annurev-cellbio-101512-122345
doi: 10.1146/annurev-cellbio-101512-122345
pubmed: 23875646
Camlin NJ, McLaughlin EA, Holt JE (2017) Motoring through: the role of kinesin superfamily proteins in female meiosis. Hum Reprod Update 23:409–420. https://doi.org/10.1093/humupd/dmx010
doi: 10.1093/humupd/dmx010
pubmed: 28431155
Kalantari S, Filges I (2020) ‘Kinesinopathies’: emerging role of the kinesin family member genes in birth defects. J Med Genet 57:797–807. https://doi.org/10.1136/jmedgenet-2019-106769
doi: 10.1136/jmedgenet-2019-106769
pubmed: 32430361
Paschal BM, Shpetner HS, Vallee R (1987) MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties. J Cell Biol 105:1273–1282. https://doi.org/10.1083/jcb.105.3.1273
doi: 10.1083/jcb.105.3.1273
pubmed: 2958482
Roberts AJ (2018) Emerging mechanisms of dynein transport in the cytoplasm versus the cilium. Biochem Soc Trans 46:967–982. https://doi.org/10.1042/BST20170568
doi: 10.1042/BST20170568
pubmed: 30065109
pmcid: 6103457
Reck-Peterson SL, Redwine WB, Vale RD, Carter AP (2018) The cytoplasmic dynein transport machinery and its many cargoes. Nat Rev Mol Cell Biol 19:382–398. https://doi.org/10.1038/s41580-018-0004-3
doi: 10.1038/s41580-018-0004-3
pubmed: 29662141
pmcid: 6457270
Schroer TA, Sheetz MP (1991) Two activators of microtubule-based vesicle transport. J Cell Biol 115:1309–1318. https://doi.org/10.1083/jcb.115.5.1309
doi: 10.1083/jcb.115.5.1309
pubmed: 1835460
Urnavicius L, Zhang K, Diamant AG, Motz C, Schlager MA, Yu M, Patel NA, Robinson CV, Carter AP (2015) The structure of the dynactin complex and its interaction with dynein. Science 347:1441–1446. https://doi.org/10.1126/science.aaa4080
doi: 10.1126/science.aaa4080
pubmed: 25814576
pmcid: 4413427
Lau CK, O’Reilly FJ, Santhanam B, Lacey SE, Rappsilber J, Carter AP (2020) Cryo-EM reveals the complex architecture of dynactin’s shoulder region and pointed end. EMBO J 40:e106164. https://doi.org/10.15252/embj.2020106164
doi: 10.15252/embj.2020106164
Urnavicius L, Lau CK, Elshenawy MM, Morales-Rios E, Motz C, Yildiz A, Carter AP (2018) Cryo-EM shows how dynactin recruits two dyneins for faster movement. Nature 554:202–206. https://doi.org/10.1038/nature25462
doi: 10.1038/nature25462
pubmed: 29420470
pmcid: 5988349
Lee IG, Cason SE, Alqassim SS, Holzbaur ELF, Dominguez R (2020) A tunable LIC1-adaptor interaction modulates dynein activity in a cargo-specific manner. Nat Commun 11:5695. https://doi.org/10.1038/s41467-020-19538-7
doi: 10.1038/s41467-020-19538-7
pubmed: 33173051
pmcid: 7655957
Celestino R, Gama JB, Castro-Rodrigues AF, Barbosa DJ, Rocha H, d’Amico EA, Musacchio A, Carvalho AX, Morais-Cabral JH, Gassmann R (2022) JIP3 interacts with dynein and kinesin-1 to regulate bidirectional organelle transport. J Cell Biol 221:e202110057. https://doi.org/10.1083/jcb.202110057
doi: 10.1083/jcb.202110057
pubmed: 35829703
pmcid: 9284427
Gama JB, Pereira C, Simões PA, Celestino R, Reis RM, Barbosa DJ, Pires HR, Carvalho C, Amorim J, Carvalho AX, Cheerambathur DK, Gassmann R (2017) Molecular mechanism of dynein recruitment to kinetochores by the Rod-Zw10-Zwilch complex and Spindly. J Cell Biol 216:943–960. https://doi.org/10.1083/jcb.201610108
doi: 10.1083/jcb.201610108
pubmed: 28320824
pmcid: 5379953
Presley JF, Cole NB, Schroer TA, Hirschberg K, Zaal KJ, Lippincott-Schwartz J (1997) ER-to-Golgi transport visualized in living cells. Nature 389:81–85. https://doi.org/10.1038/38001
doi: 10.1038/38001
pubmed: 9288971
Koushika SP, Schaefer AM, Vincent R, Willis JH, Bowerman B, Nonet ML (2004) Mutations in Caenorhabditis elegans cytoplasmic dynein components reveal specificity of neuronal retrograde cargo. J Neurosci 24:3907–3916. https://doi.org/10.1523/jneurosci.5039-03.2004
doi: 10.1523/jneurosci.5039-03.2004
pubmed: 15102906
pmcid: 6729415
Roberts AJ, Kon T, Knight PJ, Sutoh K, Burgess SA (2013) Functions and mechanics of dynein motor proteins. Nat Rev Mol Cell Biol 14:713–726. https://doi.org/10.1038/nrm3667
doi: 10.1038/nrm3667
pubmed: 24064538
pmcid: 3972880
Simons M, Nave K-A (2015) Oligodendrocytes: myelination and axonal support. Cold Spring Harb Perspect Biol 8:a020479. https://doi.org/10.1101/cshperspect.a020479
doi: 10.1101/cshperspect.a020479
pubmed: 26101081
Yang ML, Shin J, Kearns CA, Langworthy MM, Snell H, Walker MB, Appel B (2015) CNS myelination requires cytoplasmic dynein function. Dev Dyn 244:134–145. https://doi.org/10.1002/dvdy.24238
doi: 10.1002/dvdy.24238
pubmed: 25488883
pmcid: 4368448
Colman DR, Kreibich G, Frey AB, Sabatini DD (1982) Synthesis and incorporation of myelin polypeptides into CNS myelin. J Cell Biol 95:598–608. https://doi.org/10.1083/jcb.95.2.598
doi: 10.1083/jcb.95.2.598
pubmed: 6183276
Fernandez-Valle C, Gorman D, Gomez AM, Bunge MB (1997) Actin plays a role in both changes in cell shape and gene- expression associated with schwann cell myelination. J Neurosci 17:241–250. https://doi.org/10.1523/jneurosci.17-01-00241.1997
doi: 10.1523/jneurosci.17-01-00241.1997
pubmed: 8987752
pmcid: 6793673
Kim H-J, DiBernardo AB, Sloane JA, Rasband MN, Solomon D, Kosaras B, Kwak SP, Vartanian TK (2006) WAVE1 is required for oligodendrocyte morphogenesis and normal CNS myelination. J Neurosci 26:5849–5859. https://doi.org/10.1523/jneurosci.4921-05.2006
doi: 10.1523/jneurosci.4921-05.2006
pubmed: 16723544
pmcid: 6675261
Musah AS, Brown TL, Jeffries MA, Shang Q, Hashimoto H, Evangelou AV, Kowalski A, Batish M, Macklin WB, Wood TL (2020) Mechanistic target of rapamycin regulates the oligodendrocyte cytoskeleton during myelination. J Neurosci 40:2993–3007. https://doi.org/10.1523/jneurosci.1434-18.2020
doi: 10.1523/jneurosci.1434-18.2020
pubmed: 32139584
pmcid: 7141876
Bacon C, Lakics V, Machesky L, Rumsby M (2007) N-WASP regulates extension of filopodia and processes by oligodendrocyte progenitors, oligodendrocytes, and Schwann cells - implications for axon ensheathment at myelination. Glia 55:844–858. https://doi.org/10.1002/glia.20505
doi: 10.1002/glia.20505
pubmed: 17405146
Bridgman PC (2015) Myosin transport and neuronal function. Reference Module in Biomedical Sciences, Elsevier, New York
Calliari A, Farías J, Puppo A, Canclini L, Mercer JA, Munroe D, Sotelo JR, Sotelo-Silveira JR (2014) Myosin Va associates with mRNA in ribonucleoprotein particles present in myelinated peripheral axons and in the central nervous system. Dev Neurobiol 74:382–396. https://doi.org/10.1002/dneu.22155
doi: 10.1002/dneu.22155
pubmed: 24272908
Engel KL, Arora A, Goering R, Lo H-YG, Taliaferro JM (2020) Mechanisms and consequences of subcellular RNA localization across diverse cell types. Traffic 21:404–418. https://doi.org/10.1111/tra.12730
doi: 10.1111/tra.12730
pubmed: 32291836
pmcid: 7304542
Martin KC, Ephrussi A (2009) mRNA localization: gene expression in the spatial dimension. Cell 136:719–730. https://doi.org/10.1016/j.cell.2009.01.044
doi: 10.1016/j.cell.2009.01.044
pubmed: 19239891
pmcid: 2819924
Duncan ID, Lunn KF, Holmgren B, Urba-Holmgren R, Brignolo-Holmes L (1992) The taiep rat: a myelin mutant with an associated oligodendrocyte microtubular defect. J Neurocytol 21:870–884. https://doi.org/10.1007/bf01191684
doi: 10.1007/bf01191684
pubmed: 1469463
Song J, Carson JH, Barbarese E, Li F-Y, Duncan ID (2003) RNA transport in oligodendrocytes from the taiep mutant rat. Mol Cell Neurosci 24:926–938. https://doi.org/10.1016/S1044-7431(03)00254-9
doi: 10.1016/S1044-7431(03)00254-9
pubmed: 14697659
Carson JH, Worboys K, Ainger K and Barbarese E (1997) Translocation of myelin basic protein mRNA in oligodendrocytes requires microtubules and kinesin. Cell Motil Cytoskeleton 38:318-28. https://doi.org/10.1002/(sici)1097-0169(1997)38:4<318::Aid-cm2>3.0.Co;2 -#
Gould R, Freund C, Palmer F, Knapp PE, Huang J, Morrison H, Feinstein DL (1999) Messenger RNAs for kinesins and dynein are located in neural processes. Biol Bull 197:259–260. https://doi.org/10.2307/1542638
doi: 10.2307/1542638
pubmed: 10573845
Gould RM, Freund CM, Palmer F, Feinstein DL (2000) Messenger RNAs located in myelin sheath assembly sites. J Neurochem 75:1834–1844. https://doi.org/10.1046/j.1471-4159.2000.0751834.x
doi: 10.1046/j.1471-4159.2000.0751834.x
pubmed: 11032872
Pogoda H-M, Sternheim N, Lyons DA, Diamond B, Hawkins TA, Woods IG, Bhatt DH, Franzini-Armstrong C, Dominguez C, Arana N, Jacobs J, Nix R, Fetcho JR, Talbot WS (2006) A genetic screen identifies genes essential for development of myelinated axons in zebrafish. Dev Biol 298:118–131. https://doi.org/10.1016/j.ydbio.2006.06.021
doi: 10.1016/j.ydbio.2006.06.021
pubmed: 16875686
Almeida R, Lyons D (2016) Oligodendrocyte development in the absence of their target axons in vivo. PLoS One 11:e0164432. https://doi.org/10.1371/journal.pone.0164432
doi: 10.1371/journal.pone.0164432
pubmed: 27716830
pmcid: 5055324
Cotter L, Ozçelik M, Jacob C, Pereira JA, Locher V, Baumann R, Relvas JB, Suter U, Tricaud N (2010) Dlg1-PTEN interaction regulates myelin thickness to prevent damaging peripheral nerve overmyelination. Science 328:1415–1418. https://doi.org/10.1126/science.1187735
doi: 10.1126/science.1187735
pubmed: 20448149
Fujikura K, Setsu T, Tanigaki K, Abe T, Kiyonari H, Terashima T, Sakisaka T (2013) Kif14 mutation causes severe brain malformation and hypomyelination. PLoS One 8:e53490. https://doi.org/10.1371/journal.pone.0053490
doi: 10.1371/journal.pone.0053490
pubmed: 23308235
pmcid: 3537622
Noseda R, Guerrero-Valero M, Alberizzi V, Previtali SC, Sherman DL, Palmisano M, Huganir RL, Nave K-A, Cuenda A, Feltri ML, Brophy PJ, Bolino A (2016) Kif13b regulates PNS and CNS myelination through the Dlg1 scaffold. PLoS Biol 14:e1002440. https://doi.org/10.1371/journal.pbio.1002440
doi: 10.1371/journal.pbio.1002440
pubmed: 27070899
pmcid: 4829179
Mathews ES, Appel B (2016) Cholesterol biosynthesis supports myelin gene expression and axon ensheathment through modulation of P13K/Akt/mTor signaling. J Neurosci 36:7628–7639. https://doi.org/10.1523/jneurosci.0726-16.2016
doi: 10.1523/jneurosci.0726-16.2016
pubmed: 27445141
pmcid: 4951573
Preston MA, Finseth LT, Bourne JN, Macklin WB (2019) A novel myelin protein zero transgenic zebrafish designed for rapid readout of in vivo myelination. Glia 67:650–667. https://doi.org/10.1002/glia.23559
doi: 10.1002/glia.23559
pubmed: 30623975
pmcid: 6555554
Herbert AL, Fu M-m, Drerup CM, Gray RS, Harty BL, Ackerman SD, O’Reilly-Pol T, Johnson SL, Nechiporuk AV, Barres BA, Monk KR (2017) Dynein/dynactin is necessary for anterograde transport of mbp mRNA in oligodendrocytes and for myelination in vivo. Proc Natl Acad Sci U S A 114:E9153–E9162. https://doi.org/10.1073/pnas.1711088114
doi: 10.1073/pnas.1711088114
pubmed: 29073112
pmcid: 5664533
Thetiot M, Freeman SA, Roux T, Dubessy A-L, Aigrot M-S, Rappeneau Q, Lejeune F-X, Tailleur J, Sol-Foulon N, Lubetzki C, Desmazieres A (2020) An alternative mechanism of early nodal clustering and myelination onset in GABAergic neurons of the central nervous system. Glia 68:1891–1909. https://doi.org/10.1002/glia.23812
doi: 10.1002/glia.23812
pubmed: 32119167
Feng Y, Walsh CA (2004) Mitotic spindle regulation by Nde1 controls cerebral cortical size. Neuron 44:279–293. https://doi.org/10.1016/j.neuron.2004.09.023
doi: 10.1016/j.neuron.2004.09.023
pubmed: 15473967
Feng Y, Olson EC, Stukenberg PT, Flanagan LA, Kirschner MW, Walsh CA (2000) LIS1 regulates CNS lamination by interacting with mNudE, a central component of the centrosome. Neuron 28:665–679. https://doi.org/10.1016/S0896-6273(00)00145-8
doi: 10.1016/S0896-6273(00)00145-8
pubmed: 11163258
Shimizu S, Ishino Y, Tohyama M, Miyata S (2018) NDE1 positively regulates oligodendrocyte morphological differentiation. Sci Rep 8:7644. https://doi.org/10.1038/s41598-018-25898-4
doi: 10.1038/s41598-018-25898-4
pubmed: 29769557
pmcid: 5955916
Myllykoski M, Eichel MA, Jung RB, Kelm S, Werner HB, Kursula P (2018) High-affinity heterotetramer formation between the large myelin-associated glycoprotein and the dynein light chain DYNLL1. J Neurochem 147:764–783. https://doi.org/10.1111/jnc.14598
doi: 10.1111/jnc.14598
pubmed: 30261098
Janssen BJC (2018) Inside-out or outside-in, a new factor in MAG-mediated signaling in the nervous system. J Neurochem 147:712–714. https://doi.org/10.1111/jnc.14597
doi: 10.1111/jnc.14597
pubmed: 30474166
Millecamps S, Julien J-P (2013) Axonal transport deficits and neurodegenerative diseases. Nat Rev Neurosci 14:161–176. https://doi.org/10.1038/nrn3380
doi: 10.1038/nrn3380
pubmed: 23361386
Guo W, Stoklund Dittlau K, Van Den Bosch L (2020) Axonal transport defects and neurodegeneration: molecular mechanisms and therapeutic implications. Semin Cell Dev Biol 99:133–150. https://doi.org/10.1016/j.semcdb.2019.07.010
doi: 10.1016/j.semcdb.2019.07.010
pubmed: 31542222
Sleigh JN, Rossor AM, Fellows AD, Tosolini AP, Schiavo G (2019) Axonal transport and neurological disease. Nat Rev Neurol 15:691–703. https://doi.org/10.1038/s41582-019-0257-2
doi: 10.1038/s41582-019-0257-2
pubmed: 31558780
Stokin GB, Goldstein LSB (2006) Linking molecular motors to Alzheimer’s disease. J Physiol Paris 99:193–200. https://doi.org/10.1016/j.jphysparis.2005.12.085
doi: 10.1016/j.jphysparis.2005.12.085
pubmed: 16459060
Yang X, Ma Z, Lian P, Xu Y, Cao X (2023) Common mechanisms underlying axonal transport deficits in neurodegenerative diseases: a mini review. Front Mol Neurosci 16:1172197. https://doi.org/10.3389/fnmol.2023.1172197
doi: 10.3389/fnmol.2023.1172197
pubmed: 37168679
pmcid: 10164940
Pickett EK, Rose J, McCrory C, McKenzie CA, King D, Smith C, Gillingwater TH, Henstridge CM, Spires-Jones TL (2018) Region-specific depletion of synaptic mitochondria in the brains of patients with Alzheimer’s disease. Acta Neuropathol 136:747–757. https://doi.org/10.1007/s00401-018-1903-2
doi: 10.1007/s00401-018-1903-2
pubmed: 30191401
pmcid: 6208730
Wang X, Su B, Lee HG, Li X, Perry G, Smith MA, Zhu X (2009) Impaired balance of mitochondrial fission and fusion in Alzheimer’s disease. J Neurosci 29:9090–9103. https://doi.org/10.1523/jneurosci.1357-09.2009
doi: 10.1523/jneurosci.1357-09.2009
pubmed: 19605646
pmcid: 2735241
Iijima-Ando K, Hearn SA, Shenton C, Gatt A, Zhao L, Iijima K (2009) Mitochondrial mislocalization underlies Abeta42-induced neuronal dysfunction in a Drosophila model of Alzheimer’s disease. PLoS One 4:e8310. https://doi.org/10.1371/journal.pone.0008310
doi: 10.1371/journal.pone.0008310
pubmed: 20016833
pmcid: 2790372
Martin L, Latypova X, Wilson CM, Magnaudeix A, Perrin ML, Yardin C, Terro F (2013) Tau protein kinases: involvement in Alzheimer’s disease. Ageing Res Rev 12:289–309. https://doi.org/10.1016/j.arr.2012.06.003
doi: 10.1016/j.arr.2012.06.003
pubmed: 22742992
Kim C, Choi H, Jung ES, Lee W, Oh S, Jeon NL, Mook-Jung I (2012) HDAC6 inhibitor blocks amyloid beta-induced impairment of mitochondrial transport in hippocampal neurons. PLoS One 7:e42983. https://doi.org/10.1371/journal.pone.0042983
doi: 10.1371/journal.pone.0042983
pubmed: 22937007
pmcid: 3425572
Qu X, Yuan FN, Corona C, Pasini S, Pero ME, Gundersen GG, Shelanski ML, Bartolini F (2017) Stabilization of dynamic microtubules by mDia1 drives Tau-dependent Aβ(1–42) synaptotoxicity. J Cell Biol 216:3161–3178. https://doi.org/10.1083/jcb.201701045
doi: 10.1083/jcb.201701045
pubmed: 28877993
pmcid: 5626542
Chu Y, Morfini GA, Langhamer LB, He Y, Brady ST, Kordower JH (2012) Alterations in axonal transport motor proteins in sporadic and experimental Parkinson’s disease. Brain 135:2058–2073. https://doi.org/10.1093/brain/aws133
doi: 10.1093/brain/aws133
pubmed: 22719003
pmcid: 4571141
Prots I, Grosch J, Brazdis RM, Simmnacher K, Veber V, Havlicek S, Hannappel C, Krach F, Krumbiegel M, Schütz O, Reis A, Wrasidlo W, Galasko DR, Groemer TW, Masliah E, Schlötzer-Schrehardt U, Xiang W, Winkler J, Winner B (2018) α-Synuclein oligomers induce early axonal dysfunction in human iPSC-based models of synucleinopathies. Proc Natl Acad Sci U S A 115:7813–7818. https://doi.org/10.1073/pnas.1713129115
doi: 10.1073/pnas.1713129115
pubmed: 29991596
pmcid: 6065020
Nicolas A, Kenna KP, Renton AE, Ticozzi N, Faghri F, Chia R, Dominov JA, Kenna BJ, Nalls MA, Keagle P, Rivera AM, van Rheenen W, Murphy NA, van Vugt J, Geiger JT, Van der Spek RA, Pliner HA, Shankaracharya SBN, Marangi G, Topp SD, Abramzon Y, Gkazi AS, Eicher JD, Kenna A, Mora G, Calvo A, Mazzini L, Riva N, Mandrioli J, Caponnetto C, Battistini S, Volanti P, La Bella V, Conforti FL, Borghero G, Messina S, Simone IL, Trojsi F, Salvi F, Logullo FO, D’Alfonso S, Corrado L, Capasso M, Ferrucci L, Moreno CAM, Kamalakaran S, Goldstein DB, Gitler AD, Harris T, Myers RM, Phatnani H, Musunuri RL, Evani US, Abhyankar A, Zody MC, Kaye J, Finkbeiner S, Wyman SK, LeNail A, Lima L, Fraenkel E, Svendsen CN, Thompson LM, Van Eyk JE, Berry JD, Miller TM, Kolb SJ, Cudkowicz M, Baxi E, Benatar M, Taylor JP, Rampersaud E, Wu G, Wuu J, Lauria G, Verde F, Fogh I, Tiloca C, Comi GP, Sorarù G, Cereda C, Corcia P, Laaksovirta H, Myllykangas L, Jansson L, Valori M, Ealing J, Hamdalla H, Rollinson S, Pickering-Brown S, Orrell RW, Sidle KC, Malaspina A, Hardy J, Singleton AB, Johnson JO, Arepalli S, Sapp PC, McKenna-Yasek D, Polak M, Asress S, Al-Sarraj S, King A, Troakes C, Vance C, de Belleroche J, Baas F, Ten Asbroek A, Muñoz-Blanco JL, Hernandez DG, Ding J, Gibbs JR, Scholz SW, Floeter MK, Campbell RH, Landi F, Bowser R, Pulst SM, Ravits JM, MacGowan DJL, Kirby J, Pioro EP, Pamphlett R, Broach J, Gerhard G, Dunckley TL, Brady CB, Kowall NW, Troncoso JC, Le Ber I, Mouzat K, Lumbroso S, Heiman-Patterson TD, Kamel F, Van Den Bosch L, Baloh RH, Strom TM, Meitinger T, Shatunov A, Van Eijk KR, de Carvalho M, Kooyman M, Middelkoop B, Moisse M, McLaughlin RL, Van Es MA, Weber M, Boylan KB, Van Blitterswijk M, Rademakers R, Morrison KE, Basak AN, Mora JS, Drory VE, Shaw PJ, Turner MR, Talbot K, Hardiman O, Williams KL, Fifita JA, Nicholson GA, Blair IP, Rouleau GA, Esteban-Pérez J, García-Redondo A, Al-Chalabi A, Rogaeva E, Zinman L, Ostrow LW, Maragakis NJ, Rothstein JD, Simmons Z, Cooper-Knock J, Brice A, Goutman SA, Feldman EL, Gibson SB, Taroni F, Ratti A, Gellera C, Van Damme P, Robberecht W, Fratta P, Sabatelli M, Lunetta C, Ludolph AC, Andersen PM, Weishaupt JH, Camu W, Trojanowski JQ, Van Deerlin VM, Brown RH Jr, van den Berg LH, Veldink JH, Harms MB, Glass JD, Stone DJ, Tienari P, Silani V, Chiò A, Shaw CE, Traynor BJ, Landers JE (2018) Genome-wide analyses identify KIF5A as a novel ALS gene. Neuron 97:1267–1288. https://doi.org/10.1016/j.neuron.2018.02.027
doi: 10.1016/j.neuron.2018.02.027
pubmed: 29566793
Soustelle L, Aimond F, López-Andrés C, Brugioti V, Raoul C, Layalle S (2023) ALS-associated KIF5A mutation causes locomotor deficits associated with cytoplasmic inclusions, alterations of neuromuscular junctions, and motor neuron loss. J Neurosci 43:8058–8072. https://doi.org/10.1523/jneurosci.0562-23.2023
doi: 10.1523/jneurosci.0562-23.2023
pubmed: 37748861
pmcid: 10669773
Hong U, Lee J, Choi S, Jang W, Kwon S (2023) Novel mutation in KIF5A gene associated with hereditary motor and sensory neuropathy and cognitive impairment: a case report and literature review. Acta Neurol Belg 123:2375–2377. https://doi.org/10.1007/s13760-023-02199-w
doi: 10.1007/s13760-023-02199-w
pubmed: 36696008
Anazawa Y, Kita T, Iguchi R, Hayashi K, Niwa S (2022) De novo mutations in KIF1A-associated neuronal disorder (KAND) dominant-negatively inhibit motor activity and axonal transport of synaptic vesicle precursors. Proc Natl Acad Sci U S A 119:e2113795119. https://doi.org/10.1073/pnas.2113795119
doi: 10.1073/pnas.2113795119
pubmed: 35917346
pmcid: 9371658
Baron DM, Fenton AR, Saez-Atienzar S, Giampetruzzi A, Sreeram A, Shankaracharya KPJ, Doocy VR, Smith NJ, Danielson EW, Andresano M, McCormack MC, Garcia J, Bercier V, Van Den Bosch L, Brent JR, Fallini C, Traynor BJ, Holzbaur ELF, Landers JE (2022) ALS-associated KIF5A mutations abolish autoinhibition resulting in a toxic gain of function. Cell Rep 39:110598. https://doi.org/10.1016/j.celrep.2022.110598
doi: 10.1016/j.celrep.2022.110598
pubmed: 35385738
pmcid: 9134378
Hoang HT, Schlager MA, Carter AP, Bullock SL (2017) DYNC1H1 mutations associated with neurological diseases compromise processivity of dynein-dynactin-cargo adaptor complexes. Proc Natl Acad Sci U S A 114:E1597-e1606. https://doi.org/10.1073/pnas.1620141114
doi: 10.1073/pnas.1620141114
pubmed: 28196890
pmcid: 5338514
Dilokthornsakul P, Valuck RJ, Nair KV, Corboy JR, Allen RR, Campbell JD (2016) Multiple sclerosis prevalence in the United States commercially insured population. Neurology 86:1014–1021. https://doi.org/10.1212/WNL.0000000000002469
doi: 10.1212/WNL.0000000000002469
pubmed: 26888980
pmcid: 4799713
Bjelobaba I, Savic D, Lavrnja I (2017) Multiple sclerosis and neuroinflammation: the overview of current and prospective therapies. Curr Pharm Des 23:693–730. https://doi.org/10.2174/1381612822666161214153108
doi: 10.2174/1381612822666161214153108
pubmed: 27981909
Forte M, Gold BG, Marracci G, Chaudhary P, Basso E, Johnsen D, Yu X, Fowlkes J, Rahder M, Stem K, Bernardi P, Bourdette D (2007) Cyclophilin D inactivation protects axons in experimental autoimmune encephalomyelitis, an animal model of multiple sclerosis. Proc Natl Acad Sci U S A 104:7558–7563. https://doi.org/10.1073/pnas.0702228104
doi: 10.1073/pnas.0702228104
pubmed: 17463082
pmcid: 1857227
Dobson R, Giovannoni G (2019) Multiple sclerosis – a review. Eur J Neurol 26:27–40. https://doi.org/10.1111/ene.13819
doi: 10.1111/ene.13819
pubmed: 30300457
Sorbara CD, Wagner NE, Ladwig A, Nikić I, Merkler D, Kleele T, Marinković P, Naumann R, Godinho L, Bareyre FM, Bishop D, Misgeld T, Kerschensteiner M (2014) Pervasive axonal transport deficits in multiple sclerosis models. Neuron 84:1183–1190. https://doi.org/10.1016/j.neuron.2014.11.006
doi: 10.1016/j.neuron.2014.11.006
pubmed: 25433639
Kiryu-Seo S, Ohno N, Kidd GJ, Komuro H, Trapp BD (2010) Demyelination increases axonal stationary mitochondrial size and the speed of axonal mitochondrial transport. J Neurosci 30:6658–6666. https://doi.org/10.1523/jneurosci.5265-09.2010
doi: 10.1523/jneurosci.5265-09.2010
pubmed: 20463228
pmcid: 2885867
Ohno N, Kidd GJ, Mahad D, Kiryu-Seo S, Avishai A, Komuro H, Trapp BD (2011) Myelination and axonal electrical activity modulate the distribution and motility of mitochondria at CNS nodes of Ranvier. J Neurosci 31:7249–7258. https://doi.org/10.1523/jneurosci.0095-11.2011
doi: 10.1523/jneurosci.0095-11.2011
pubmed: 21593309
pmcid: 3139464
Edgar JM, McLaughlin M, Yool D, Zhang SC, Fowler JH, Montague P, Barrie JA, McCulloch MC, Duncan ID, Garbern J, Nave KA, Griffiths IR (2004) Oligodendroglial modulation of fast axonal transport in a mouse model of hereditary spastic paraplegia. J Cell Biol 166:121–131. https://doi.org/10.1083/jcb.200312012
doi: 10.1083/jcb.200312012
pubmed: 15226307
pmcid: 2172145
Yin X, Kidd GJ, Ohno N, Perkins GA, Ellisman MH, Bastian C, Brunet S, Baltan S, Trapp BD (2016) Proteolipid protein-deficient myelin promotes axonal mitochondrial dysfunction via altered metabolic coupling. J Cell Biol 215:531–542. https://doi.org/10.1083/jcb.201607099
doi: 10.1083/jcb.201607099
pubmed: 27872255
pmcid: 5119941
Priller C, Bauer T, Mitteregger G, Krebs B, Kretzschmar HA, Herms J (2006) Synapse formation and function is modulated by the amyloid precursor protein. J Neurosci 26:7212–7221. https://doi.org/10.1523/jneurosci.1450-06.2006
doi: 10.1523/jneurosci.1450-06.2006
pubmed: 16822978
pmcid: 6673945
Ferguson B, Matyszak MK, Esiri MM, Perry VH (1997) Axonal damage in acute multiple sclerosis lesions. Brain 120:393–399. https://doi.org/10.1093/brain/120.3.393
doi: 10.1093/brain/120.3.393
pubmed: 9126051
Kuhlmann T, Lingfeld G, Bitsch A, Schuchardt J, Brück W (2002) Acute axonal damage in multiple sclerosis is most extensive in early disease stages and decreases over time. Brain 125:2202–2212. https://doi.org/10.1093/brain/awf235
doi: 10.1093/brain/awf235
pubmed: 12244078
Sharief MK, Hentges R (1991) Association between tumor necrosis factor-alpha and disease progression in patients with multiple sclerosis. N Engl J Med 325:467–472. https://doi.org/10.1056/nejm199108153250704
doi: 10.1056/nejm199108153250704
pubmed: 1852181
Petrache I, Birukova A, Ramirez SI, Garcia JG, Verin AD (2003) The role of the microtubules in tumor necrosis factor-alpha-induced endothelial cell permeability. Am J Respir Cell Mol Biol 28:574–581. https://doi.org/10.1165/rcmb.2002-0075OC
doi: 10.1165/rcmb.2002-0075OC
pubmed: 12707013
Vancompernolle K, Boonefaes T, Mann M, Fiers W, Grooten J (2000) Tumor necrosis factor-induced microtubule stabilization mediated by hyperphosphorylated oncoprotein 18 promotes cell death. J Biol Chem 275:33876–33882. https://doi.org/10.1074/jbc.M004785200
doi: 10.1074/jbc.M004785200
pubmed: 10913145
Shivanna M, Srinivas SP (2009) Microtubule stabilization opposes the (TNF-alpha)-induced loss in the barrier integrity of corneal endothelium. Exp Eye Res 89:950–959. https://doi.org/10.1016/j.exer.2009.08.004
doi: 10.1016/j.exer.2009.08.004
pubmed: 19695246
pmcid: 2784278
Stagi M, Gorlovoy P, Larionov S, Takahashi K, Neumann H (2006) Unloading kinesin transported cargoes from the tubulin track via the inflammatory c-Jun N-terminal kinase pathway. Faseb J 20:2573–2575. https://doi.org/10.1096/fj.06-6679fje
doi: 10.1096/fj.06-6679fje
pubmed: 17068110
Olmos G, Lladó J (2014) Tumor necrosis factor alpha: a link between neuroinflammation and excitotoxicity. Mediators Inflamm 2014:861231. https://doi.org/10.1155/2014/861231
doi: 10.1155/2014/861231
pubmed: 24966471
pmcid: 4055424
Trapp BD, Stys PK (2009) Virtual hypoxia and chronic necrosis of demyelinated axons in multiple sclerosis. Lancet Neurol 8:280–291. https://doi.org/10.1016/s1474-4422(09)70043-2
doi: 10.1016/s1474-4422(09)70043-2
pubmed: 19233038
Mattson MP, Engle MG, Rychlik B (1991) Effects of elevated intracellular calcium levels on the cytoskeleton and tau in cultured human cortical neurons. Mol Chem Neuropathol 15:117–142. https://doi.org/10.1007/bf03159951
doi: 10.1007/bf03159951
pubmed: 1663746
Chung RS, McCormack GH, King AE, West AK, Vickers JC (2005) Glutamate induces rapid loss of axonal neurofilament proteins from cortical neurons in vitro. Exp Neurol 193:481–488. https://doi.org/10.1016/j.expneurol.2005.01.005
doi: 10.1016/j.expneurol.2005.01.005
pubmed: 15869950
Witte ME, Schumacher AM, Mahler CF, Bewersdorf JP, Lehmitz J, Scheiter A, Sánchez P, Williams PR, Griesbeck O, Naumann R, Misgeld T, Kerschensteiner M (2019) Calcium influx through plasma-membrane nanoruptures drives axon degeneration in a model of multiple sclerosis. Neuron 101:615–624. https://doi.org/10.1016/j.neuron.2018.12.023
doi: 10.1016/j.neuron.2018.12.023
pubmed: 30686733
pmcid: 6389591
Hiruma H, Katakura T, Takahashi S, Ichikawa T, Kawakami T (2003) Glutamate and amyloid beta-protein rapidly inhibit fast axonal transport in cultured rat hippocampal neurons by different mechanisms. J Neurosci 23:8967–8977. https://doi.org/10.1523/jneurosci.23-26-08967.2003
doi: 10.1523/jneurosci.23-26-08967.2003
pubmed: 14523099
pmcid: 6740390
Chang KT, Niescier RF, Min KT (2011) Mitochondrial matrix Ca2+ as an intrinsic signal regulating mitochondrial motility in axons. Proc Natl Acad Sci U S A 108:15456–15461. https://doi.org/10.1073/pnas.1106862108
doi: 10.1073/pnas.1106862108
pubmed: 21876166
pmcid: 3174631
Wang X, Schwarz TL (2009) The mechanism of Ca
doi: 10.1016/j.cell.2008.11.046
pubmed: 19135897
pmcid: 2768392
Dutta R, McDonough J, Yin X, Peterson J, Chang A, Torres T, Gudz T, Macklin WB, Lewis DA, Fox RJ, Rudick R, Mirnics K, Trapp BD (2006) Mitochondrial dysfunction as a cause of axonal degeneration in multiple sclerosis patients. Ann Neurol 59:478–489. https://doi.org/10.1002/ana.20736
doi: 10.1002/ana.20736
pubmed: 16392116
Geurts JJ, Barkhof F (2008) Grey matter pathology in multiple sclerosis. Lancet Neurol 7:841–851. https://doi.org/10.1016/s1474-4422(08)70191-1
doi: 10.1016/s1474-4422(08)70191-1
pubmed: 18703006
Kostic M, Zivkovic N, Stojanovic I (2013) Multiple sclerosis and glutamate excitotoxicity. Rev Neurosci 24:71–88. https://doi.org/10.1515/revneuro-2012-0062
doi: 10.1515/revneuro-2012-0062
pubmed: 23152401
Kuzmina US, Zainullina LF, Vakhitov VA, Bakhtiyarova KZ, Vakhitova YV (2020) The role of glutamate in the pathogenesis of multiple sclerosis. Neurosci Behav Physiol 50:669–675. https://doi.org/10.1007/s11055-020-00953-8
doi: 10.1007/s11055-020-00953-8
Macrez R, Stys PK, Vivien D, Lipton SA, Docagne F (2016) Mechanisms of glutamate toxicity in multiple sclerosis: biomarker and therapeutic opportunities. Lancet Neurol 15:1089–1102. https://doi.org/10.1016/s1474-4422(16)30165-x
doi: 10.1016/s1474-4422(16)30165-x
pubmed: 27571160
Ikegami K, Setou M (2010) Unique post-translational modifications in specialized microtubule architecture. Cell Struct Funct 35:15–22. https://doi.org/10.1247/csf.09027
doi: 10.1247/csf.09027
pubmed: 20190462
Janke C, Bulinski JC (2011) Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions. Nat Rev Mol Cell Biol 12:773–786. https://doi.org/10.1038/nrm3227
doi: 10.1038/nrm3227
pubmed: 22086369
Sirajuddin M, Rice LM, Vale RD (2014) Regulation of microtubule motors by tubulin isotypes and post-translational modifications. Nat Cell Biol 16:335–344. https://doi.org/10.1038/ncb2920
doi: 10.1038/ncb2920
pubmed: 24633327
pmcid: 4117587
Bär J, Popp Y, Bucher M, Mikhaylova M (2022) Direct and indirect effects of tubulin post-translational modifications on microtubule stability: insights and regulations. Biochim Biophys Acta Mol Cell Res 1869:119241. https://doi.org/10.1016/j.bbamcr.2022.119241
doi: 10.1016/j.bbamcr.2022.119241
pubmed: 35181405
Hammond JW, Huang CF, Kaech S, Jacobson C, Banker G, Verhey KJ (2010) Posttranslational modifications of tubulin and the polarized transport of kinesin-1 in neurons. Mol Biol Cell 21:572–583. https://doi.org/10.1091/mbc.e09-01-0044
doi: 10.1091/mbc.e09-01-0044
pubmed: 20032309
pmcid: 2820422
Kaul N, Soppina V, Verhey KJ (2014) Effects of α-tubulin K40 acetylation and detyrosination on kinesin-1 motility in a purified system. Biophys J 106:2636–2643. https://doi.org/10.1016/j.bpj.2014.05.008
doi: 10.1016/j.bpj.2014.05.008
pubmed: 24940781
pmcid: 4070028
Reed NA, Cai D, Blasius TL, Jih GT, Meyhofer E, Gaertig J, Verhey KJ (2006) Microtubule acetylation promotes kinesin-1 binding and transport. Curr Biol 16:2166–2172. https://doi.org/10.1016/j.cub.2006.09.014
doi: 10.1016/j.cub.2006.09.014
pubmed: 17084703
Stroissnigg H, Trancíková A, Descovich L, Fuhrmann J, Kutschera W, Kostan J, Meixner A, Nothias F, Propst F (2007) S-nitrosylation of microtubule-associated protein 1B mediates nitric-oxide-induced axon retraction. Nat Cell Biol 9:1035–1045. https://doi.org/10.1038/ncb1625
doi: 10.1038/ncb1625
pubmed: 17704770
Sun J, Zhou H, Bai F, Ren Q, Zhang Z (2016) Myelin injury induces axonal transport impairment but not AD-like pathology in the hippocampus of cuprizone-fed mice. Oncotarget 7:30003–17. https://doi.org/10.18632/oncotarget.8981
doi: 10.18632/oncotarget.8981
pubmed: 27129150
pmcid: 5058659
Lee JY, Kim MJ, Thomas S, Oorschot V, Ramm G, Aui PM, Sekine Y, Deliyanti D, Wilkinson-Berka J, Be N, Harvey AR, Theotokis P, McLean C, Strittmatter SM, Petratos S (2019) Limiting neuronal nogo receptor 1 signaling during experimental autoimmune encephalomyelitis preserves axonal transport and abrogates inflammatory demyelination. J Neurosci 39:5562–5580. https://doi.org/10.1523/jneurosci.1760-18.2019
doi: 10.1523/jneurosci.1760-18.2019
pubmed: 31061088
pmcid: 6616297
Szolnoki Z, Kondacs A, Mandi Y, Somogyvari F (2007) A cytoskeleton motor protein genetic variant may exert a protective effect on the occurrence of multiple sclerosis: the janus face of the kinesin light-chain 1 56836CC genetic variant. Neuromolecular Med 9:335–339. https://doi.org/10.1007/s12017-007-8014-x
doi: 10.1007/s12017-007-8014-x
pubmed: 17999208
Aulchenko YS, Hoppenbrouwers IA, Ramagopalan SV, Broer L, Jafari N, Hillert J, Link J, Lundström W, Greiner E, Dessa Sadovnick A, Goossens D, Van Broeckhoven C, Del-Favero J, Ebers GC, Oostra BA, van Duijn CM, Hintzen RQ (2008) Genetic variation in the KIF1B locus influences susceptibility to multiple sclerosis. Nat Genet 40:1402–1403. https://doi.org/10.1038/ng.251
doi: 10.1038/ng.251
pubmed: 18997785
Booth DR, Heard RN, Stewart GJ, Cox M, Scott RJ, Lechner-Scott J, Goris A, Dobosi R, Dubois B, Saarela J, Leppä V, Peltonen L, Pirttila T, Cournu-Rebeix I, Fontaine B, Bergamaschi L, D’Alfonso S, Leone M, Lorentzen AR, Harbo HF, Celius EG, Spurkland A, Link J, Kockum I, Olsson T, Hillert J, Ban M, Baker A, Kemppinen A, Sawcer S, Compston A, Robertson NP, De Jager PL, Hafler DA, Barcellos LF, Ivinson AJ, McCauley JL, Pericak-Vance MA, Oksenberg JR, Hauser SL, Sexton D and Haines J (2010) Lack of support for association between the KIF1B rs10492972[C] variant and multiple sclerosis. Nat Genet 42:469–70; author reply 470–1. https://doi.org/10.1038/ng0610-469
Martinelli-Boneschi F, Esposito F, Scalabrini D, Fenoglio C, Rodegher ME, Brambilla P, Colombo B, Ghezzi A, Capra R, Collimedaglia L, Coniglio G, De Riz M, Serpente M, Cantoni C, Scarpini E, Martinelli V, Galimberti D, Comi G (2010) Lack of replication of KIF1B gene in an Italian primary progressive multiple sclerosis cohort. Eur J Neurol 17:740–745. https://doi.org/10.1111/j.1468-1331.2009.02925.x
doi: 10.1111/j.1468-1331.2009.02925.x
pubmed: 20067515
Kudryavtseva EA, Rozhdestvenskii AS, Kakulya AV, Khanokh EV, Delov RA, Malkova NA, Korobko DS, Platonov FA, Aref′eva EG, Zagorskaya NN, Aliferova VM, Titova MA, Babenko SA, Smagina IV, El′chaninova SA, Zolovkina AG, Lifshits GI, Puzyrev VP, Filipenko ML (2011) Polymorphic locus rs10492972 of the KIF1B gene association with multiple sclerosis in Russia: case control study. Mol Genet Metab 104:390–394. https://doi.org/10.1016/j.ymgme.2011.05.018
doi: 10.1016/j.ymgme.2011.05.018
pubmed: 21680216
Bahlo M, Booth DR, Broadley SA, Brown MA, Foote SJ, Griffiths LR, Kilpatrick TJ, Lechner-Scott J, Moscato P, Perreau VM, Rubio JP, Scott RJ, Stankovich J, Stewart GJ, Taylor BV, Wiley J, Brown MA, Booth DR, Clarke G, Cox MB, Csurhes PA, Danoy P, Drysdale K, Field J, Foote SJ, Greer JM, Griffiths LR, Guru P, Hadler J, McMorran BJ, Jensen CJ, Johnson LJ, McCallum R, Merriman M, Merriman T, Pryce K, Scott RJ, Stewart GJ, Tajouri L, Wilkins EJ, Rubio JP, Bahlo M, Brown MA, Browning BL, Browning SR, Perera D, Rubio JP, Stankovich J, Broadley S, Butzkueven H, Carroll WM, Chapman C, Kermode AG, Marriott M, Mason D, Heard RN, Pender MP, Slee M, Tubridy N, Lechner-Scott J, Taylor BV, Willoughby E, Kilpatrick TJ (2009) Genome-wide association study identifies new multiple sclerosis susceptibility loci on chromosomes 12 and 20. Nat Genet 41:824–828. https://doi.org/10.1038/ng.396
doi: 10.1038/ng.396
Koutsis G, Karadima G, Floroskufi P, Sfagos C, Vassilopoulos D, Panas M (2011) The rs10492972 KIF1B polymorphism and disease progression in Greek patients with multiple sclerosis. J Neurol 258:1726–1728. https://doi.org/10.1007/s00415-011-6004-2
doi: 10.1007/s00415-011-6004-2
pubmed: 21424745
Consortium TIMSG (2009) Comprehensive follow-up of the first genome-wide association study of multiple sclerosis identifies KIF21B and TMEM39A as susceptibility loci. Hum Mol Genet 19:953–962. https://doi.org/10.1093/hmg/ddp542
doi: 10.1093/hmg/ddp542
Goris A, Boonen S, D’hooghe M-B, Dubois B (2010) Replication of KIF21B as a susceptibility locus for multiple sclerosis. J Med Genet 47:775–776. https://doi.org/10.1136/jmg.2009.075911
doi: 10.1136/jmg.2009.075911
pubmed: 20587413
Alcina A, Vandenbroeck K, Otaegui D, Saiz A, Gonzalez JR, Fernandez O, Cavanillas ML, Cénit MC, Arroyo R, Alloza I, García-Barcina M, Antigüedad A, Leyva L, Izquierdo G, Lucas M, Fedetz M, Pinto-Medel MJ, Olascoaga J, Blanco Y, Comabella M, Montalban X, Urcelay E, Matesanz F (2010) The autoimmune disease-associated KIF5A, CD226 and SH2B3 gene variants confer susceptibility for multiple sclerosis. Genes Immun 11:439–445. https://doi.org/10.1038/gene.2010.30
doi: 10.1038/gene.2010.30
pubmed: 20508602
Mohan N, Sorokina EM, Verdeny IV, Alvarez AS, Lakadamyali M (2019) Detyrosinated microtubules spatially constrain lysosomes facilitating lysosome-autophagosome fusion. J Cell Biol 218:632–643. https://doi.org/10.1083/jcb.201807124
doi: 10.1083/jcb.201807124
pubmed: 30567713
pmcid: 6363446
Chen R, Tang X, Zhao Y, Shen Z, Zhang M, Shen Y, Li T, Chung CHY, Zhang L, Wang J, Cui B, Fei P, Guo Y, Du S, Yao S (2023) Single-frame deep-learning super-resolution microscopy for intracellular dynamics imaging. Nat Commun 14:2854. https://doi.org/10.1038/s41467-023-38452-2
doi: 10.1038/s41467-023-38452-2
pubmed: 37202407
pmcid: 10195829
Singh K, Lau CK, Manigrasso G, Gama JB, Gassmann R, Carter AP (2024) Molecular mechanism of dynein-dynactin complex assembly by LIS1. Science 383:eadk8544. https://doi.org/10.1126/science.adk8544
doi: 10.1126/science.adk8544
pubmed: 38547289
pmcid: 7615804
Chaaban S, Carter AP (2022) Structure of dynein-dynactin on microtubules shows tandem adaptor binding. Nature 610:212–216. https://doi.org/10.1038/s41586-022-05186-y
doi: 10.1038/s41586-022-05186-y
pubmed: 36071160
Benoit M, Rao L, Asenjo AB, Gennerich A, Sosa H (2024) Cryo-EM unveils kinesin KIF1A’s processivity mechanism and the impact of its pathogenic variant P305L. Nat Commun 15:5530. https://doi.org/10.1038/s41467-024-48720-4
doi: 10.1038/s41467-024-48720-4
pubmed: 38956021
pmcid: 11219953
McMillan SN, Scarff CA (2022) Cryo-electron microscopy analysis of myosin at work and at rest. Curr Opin Struct Biol 75:102391. https://doi.org/10.1016/j.sbi.2022.102391
doi: 10.1016/j.sbi.2022.102391
pubmed: 35636003
Jurriens D, van Batenburg V, Katrukha EA, Kapitein LC (2021) Mapping the neuronal cytoskeleton using expansion microscopy. Methods Cell Biol 161:105–124. https://doi.org/10.1016/bs.mcb.2020.04.018
doi: 10.1016/bs.mcb.2020.04.018
pubmed: 33478685
Klimas A, Gallagher BR, Wijesekara P, Fekir S, DiBernardo EF, Cheng Z, Stolz DB, Cambi F, Watkins SC, Brody SL, Horani A, Barth AL, Moore CI, Ren X, Zhao Y (2023) Magnify is a universal molecular anchoring strategy for expansion microscopy. Nat Biotechnol 41:858–869. https://doi.org/10.1038/s41587-022-01546-1
doi: 10.1038/s41587-022-01546-1
pubmed: 36593399
pmcid: 10264239