Following the Dynamism of the Mitochondrial Network in T Cells.
Dynamic network
Fission
Fusion
Imaging
Mitochondria
Morphology
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2021
2021
Historique:
entrez:
7
6
2021
pubmed:
8
6
2021
medline:
11
8
2021
Statut:
ppublish
Résumé
The dynamism of mitochondria, considered as complex and motile organelles, is brought about by mitochondria ability to undergo cycles of fission and fusion events, whose fine balance determines their morphology in a specific physiological context. A huge body of evidence makes it possible to associate mitochondrial organization to regulation of an increasing number of key cellular processes, such as biosynthetic pathways, oxidative phosphorylation and ATP production, calcium buffering, mtDNA homeostasis, autophagy, and cell death. Here, we review the recently developed imaging methods for studying mitochondrial dynamics, including live-cell imaging, by using mitochondrial-targeted fluorescent proteins. In more details, we focus our attention on two different protocols in the T cell model, an example of nonadherent cells, which present some particularities and difficulties in the analysis of mitochondrial shape. Also, we discuss some examples of mouse models carrying mitochondria-targeted fluorescent proteins, which allow to investigate the mitochondrial morphology in vivo.
Identifiants
pubmed: 34096009
doi: 10.1007/978-1-0716-1433-4_16
doi:
Substances chimiques
Fluorescent Dyes
0
Luminescent Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
287-299Références
Seo AY, Joseph A-M, Dutta D, Hwang JCY, Aris JP, Leeuwenburgh C (2010) New insights into the role of mitochondria in aging: mitochondrial dynamics and more. J Cell Sci 123:2533–2542. https://doi.org/10.1242/jcs.070490
doi: 10.1242/jcs.070490
pubmed: 20940129
pmcid: 2912461
van der Bliek AM, Shen Q, Kawajiri S (2013) Mechanisms of mitochondrial fission and fusion. Cold Spring Harb Perspect Biol 5:a011072. https://doi.org/10.1101/cshperspect.a011072
doi: 10.1101/cshperspect.a011072
pubmed: 23732471
pmcid: 3660830
Ito YA, Di Polo A (2017) Mitochondrial dynamics, transport, and quality control: a bottleneck for retinal ganglion cell viability in optic neuropathies. Mitochondrion 36:186–192. https://doi.org/10.1016/j.mito.2017.08.014
doi: 10.1016/j.mito.2017.08.014
pubmed: 28866056
Corrado M, Scorrano L, Campello S (2012) Mitochondrial dynamics in cancer and neurodegenerative and neuroinflammatory diseases. Int J Cell Biol 2012:1–13. https://doi.org/10.1155/2012/729290
doi: 10.1155/2012/729290
Twig G, Hyde B, Shirihai OS (2008) Mitochondrial fusion, fission and autophagy as a quality control axis: the bioenergetic view. Biochim Biophys Acta Bioenerg 1777:1092–1097. https://doi.org/10.1016/j.bbabio.2008.05.001
doi: 10.1016/j.bbabio.2008.05.001
Buck MD, O’Sullivan D, Klein Geltink RI, Curtis JD, Chang CH, Sanin DE, Qiu J, Kretz O, Braas D, van der Windt GJ, Chen Q, Huang SC, O’Neill CM, Edelson BT, Pearce EJL, Sesaki H, Huber TB, Rambold AS, Pearce EJL (2016) Mitochondrial dynamics controls T cell fate through metabolic programming. Cell 166:63–76. https://doi.org/10.1016/j.cell.2016.05.035
doi: 10.1016/j.cell.2016.05.035
pubmed: 27293185
pmcid: 4974356
Kingnate C, Charoenkwan K, Kumfu S, Chattipakorn N, Chattipakorn SC (2018) Possible roles of mitochondrial dynamics and the effects of pharmacological interventions in chemoresistant ovarian cancer. EBioMedicine 34:256–266. https://doi.org/10.1016/j.ebiom.2018.07.026
doi: 10.1016/j.ebiom.2018.07.026
pubmed: 30049609
pmcid: 6116427
da Silva AF, Mariotti FR, Máximo V, Campello S (2014) Mitochondria dynamism: of shape, transport and cell migration. Cell Mol Life Sci 71(12):2313–2324. https://doi.org/10.1007/s00018-014-1557-8
doi: 10.1007/s00018-014-1557-8
pubmed: 24442478
Junker C, Hoth M (2011) Immune synapses: mitochondrial morphology matters. EMBO J 30:1187–1189. https://doi.org/10.1038/emboj.2011.72
doi: 10.1038/emboj.2011.72
pubmed: 21468096
pmcid: 3094123
Mishra P, Chan DC (2014) Mitochondrial dynamics and inheritance during cell division, development and disease. Nat Rev Mol Cell Biol 15:634–646. https://doi.org/10.1038/nrm3877
doi: 10.1038/nrm3877
pubmed: 25237825
pmcid: 4250044
Tilokani L, Nagashima S, Paupe V, Prudent J (2018) Mitochondrial dynamics: overview of molecular mechanisms. Essays Biochem 62:341–360. https://doi.org/10.1042/EBC20170104
doi: 10.1042/EBC20170104
pubmed: 30030364
pmcid: 6056715
Ong S-B, Hall AR, Hausenloy DJ (2013) Mitochondrial dynamics in cardiovascular health and disease. Antioxid Redox Signal 19:400–414. https://doi.org/10.1089/ars.2012.4777
doi: 10.1089/ars.2012.4777
pubmed: 22793879
pmcid: 3699895
Smirnova E, Griparic L, Shurland D-L, van der Bliek AM (2001) Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol Biol Cell 12:2245–2256. https://doi.org/10.1091/mbc.12.8.2245
doi: 10.1091/mbc.12.8.2245
pubmed: 11514614
pmcid: 58592
Otera H, Wang C, Cleland MM, Setoguchi K, Yokota S, Youle RJ, Mihara K (2010) Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells. J Cell Biol 191:1141–1158. https://doi.org/10.1083/jcb.201007152
doi: 10.1083/jcb.201007152
pubmed: 21149567
pmcid: 3002033
Liu R, Chan DC (2015) The mitochondrial fission receptor Mff selectively recruits oligomerized Drp1. Mol Biol Cell 26:4466–4477. https://doi.org/10.1091/mbc.E15-08-0591
doi: 10.1091/mbc.E15-08-0591
pubmed: 26446846
pmcid: 4666140
Zhao J, Liu T, Jin S, Wang X, Qu M, Uhlén P, Tomilin N, Shupliakov O, Lendahl U, Nistér M (2011) Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission. EMBO J 30:2762–2778. https://doi.org/10.1038/emboj.2011.198
doi: 10.1038/emboj.2011.198
pubmed: 21701560
pmcid: 3160255
Lee H, Yoon Y (2014) Mitochondrial fission: regulation and ER connection. Mol Cells 37:89–94. https://doi.org/10.14348/molcells.2014.2329
doi: 10.14348/molcells.2014.2329
pubmed: 24598992
pmcid: 3935634
Alarcón B, Mestre D, Martínez-Martín N (2011) The immunological synapse: a cause or consequence of T-cell receptor triggering? Immunology 133:420–425. https://doi.org/10.1111/j.1365-2567.2011.03458.x
doi: 10.1111/j.1365-2567.2011.03458.x
pubmed: 21631496
pmcid: 3143353
Contento RL, Campello S, Trovato AE, Magrini E, Anselmi F, Viola A (2010) Adhesion shapes T cells for prompt and sustained T-cell receptor signalling. EMBO J 29:4035–4047. https://doi.org/10.1038/emboj.2010.258
doi: 10.1038/emboj.2010.258
pubmed: 20953162
pmcid: 3020646
Simula L, Pacella I, Colamatteo A, Procaccini C, Cancila V, Bordi M, Tregnago C, Corrado M, Pigazzi M, Barnaba V, Tripodo C, Matarese G, Piconese S, Campello S (2018) Drp1 controls effective T cell immune-surveillance by regulating T cell migration, proliferation, and cMyc-dependent metabolic reprogramming. Cell Rep 25:3059–3073. https://doi.org/10.1016/j.celrep.2018.11.018
doi: 10.1016/j.celrep.2018.11.018
pubmed: 30540939
pmcid: 6302735
Campello S, Lacalle RA, Bettella M, Mañes S, Scorrano L, Viola A (2006) Orchestration of lymphocyte chemotaxis by mitochondrial dynamics. J Exp Med 203:2879–2886. https://doi.org/10.1084/jem.20061877
doi: 10.1084/jem.20061877
pubmed: 17145957
pmcid: 2118173
Simula L, Nazio F, Campello S (2017) The Mitochondrial dynamics in cancer and immune-surveillance. Semin Cancer Biol 47:29–42. https://doi.org/10.1016/j.semcancer.2017.06.007
doi: 10.1016/j.semcancer.2017.06.007
pubmed: 28655520
Wang R, Dillon CPP, Shi LZZ, Milasta S, Carter R, Finkelstein D, McCormick LLL, Fitzgerald P, Chi H, Munger J, Green DRR (2011) The transcription factor Myc controls metabolic reprogramming upon T lymphocyte activation. Immunity 35:871–882. https://doi.org/10.1016/j.immuni.2011.09.021
doi: 10.1016/j.immuni.2011.09.021
pubmed: 22195744
pmcid: 3248798
Simula L, Campanella M, Campello S (2019) Targeting Drp1 and mitochondrial fission for therapeutic immune modulation. Pharmacol Res 146:104317. https://doi.org/10.1016/J.PHRS.2019.104317
doi: 10.1016/J.PHRS.2019.104317
pubmed: 31220561
Scaduto RC, Grotyohann LW (1999) Measurement of mitochondrial membrane potential using fluorescent rhodamine derivatives. Biophys J 76:469–477. https://doi.org/10.1016/S0006-3495(99)77214-0
doi: 10.1016/S0006-3495(99)77214-0
pubmed: 9876159
pmcid: 1302536
Perry SW, Norman JP, Barbieri J, Brown EB, Gelbard HA (2011) Mitochondrial membrane potential probes and the proton gradient: a practical usage guide. Biotechniques 50:98–115. https://doi.org/10.2144/000113610
doi: 10.2144/000113610
pubmed: 21486251
pmcid: 3115691
Sorvina A, Bader CA, Darby JRT, Lock MC, Soo JY, Johnson IRD, Caporale C, Voelcker NH, Stagni S, Massi M, Morrison JL, Plush SE, Brooks DA (2018) Mitochondrial imaging in live or fixed tissues using a luminescent iridium complex. Sci Rep 8:8191. https://doi.org/10.1038/s41598-018-24672-w
doi: 10.1038/s41598-018-24672-w
pubmed: 29844412
pmcid: 5974328
Liu X, Yang L, Long Q, Weaver D, Hajnóczky G (2017) Choosing proper fluorescent dyes, proteins, and imaging techniques to study mitochondrial dynamics in mammalian cells. Biophys Rep 3:64–72. https://doi.org/10.1007/s41048-017-0037-8
doi: 10.1007/s41048-017-0037-8
pubmed: 29238743
pmcid: 5719805
Lukyanov KA, Chudakov DM, Lukyanov S, Verkhusha VV (2005) Photoactivatable fluorescent proteins. Nat Rev Mol Cell Biol 6(11):885–891
doi: 10.1038/nrm1741
Shitara H, Shimanuki M, Jun-Ichi H, Yonekawa H (2010) Global imaging of mitochondrial morphology in tissues using transgenic mice expressing mitochondrially targeted enhanced green fluorescent protein. Exp Anim 59:99–103. https://doi.org/10.1538/expanim.59.99
doi: 10.1538/expanim.59.99
pubmed: 20224174
Barrasso AP, Tong X, Poché RA (2018) The mito::mKate2 mouse: a far-red fluorescent reporter mouse line for tracking mitochondrial dynamics in vivo. Genesis 56:e23087. https://doi.org/10.1002/dvg.23087
doi: 10.1002/dvg.23087
Sterky FH, Lee S, Wibom R, Olson L, Larsson NG (2011) Impaired mitochondrial transport and Parkin-independent degeneration of respiratory chain-deficient dopamine neurons in vivo. Proc Natl Acad Sci U S A 108:12937–12942. https://doi.org/10.1073/pnas.1103295108
doi: 10.1073/pnas.1103295108
pubmed: 21768369
pmcid: 3150929