Functional maintenance of calcium store by ShcB adaptor protein in cerebellar Purkinje cells.

Animals Calcium / metabolism Calcium Signaling / genetics Cerebellum / metabolism Endoplasmic Reticulum / genetics Humans Long-Term Synaptic Depression / genetics Mice Mice, Knockout Motor Disorders / genetics Neuronal Plasticity / genetics Purkinje Cells / metabolism Sarcoplasmic Reticulum Calcium-Transporting ATPases / genetics Src Homology 2 Domain-Containing, Transforming Protein 2 / genetics Synapses / genetics

Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
02 09 2020
Historique:
received: 18 04 2020
accepted: 14 08 2020
entrez: 4 9 2020
pubmed: 4 9 2020
medline: 25 2 2021
Statut: epublish

Résumé

Intracellular Ca

Identifiants

DOI: 10.1038/s41598-020-71414-y PMID: 32879382 PMC: PMC7468156
pubmed: 32879382
doi: 10.1038/s41598-020-71414-y
pii: 10.1038/s41598-020-71414-y
pmc: PMC7468156
doi:

Substances chimiques

Src Homology 2 Domain-Containing, Transforming Protein 2 0
Sarcoplasmic Reticulum Calcium-Transporting ATPases EC 3.6.3.8
Calcium SY7Q814VUP

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

14475

Références

Berridge, M. J. The endoplasmic reticulum: a multifunctional signaling organelle. Cell Calcium 32, 235–249. https://doi.org/10.1016/s0143-4160(023)00182-3 (2002).
doi: 10.1016/s0143-4160(023)00182-3 pubmed: 12543086
Berridge, M. J., Lipp, P. & Bootman, M. D. The versatility and universality of calcium signalling. Nat. Rev. Mol. Cell Biol. 1, 11–21. https://doi.org/10.1038/35036035 (2000).
doi: 10.1038/35036035 pubmed: 11413485
Clapham, D. E. Calcium signaling. Cell 131, 1047–1058. https://doi.org/10.1016/j.cell.2007.11.028 (2007).
doi: 10.1016/j.cell.2007.11.028 pubmed: 18083096
Mattson, M. P. et al. Calcium signaling in the ER: its role in neuronal plasticity and neurodegenerative disorders. Trends Neurosci. 23, 222–229. https://doi.org/10.1016/s0166-2236(00)01548-4 (2000).
doi: 10.1016/s0166-2236(00)01548-4 pubmed: 10782128
Paschen, W. & Mengesdorf, T. Endoplasmic reticulum stress response and neurodegeneration. Cell Calcium 38, 409–415. https://doi.org/10.1016/j.ceca.2005.06.019 (2005).
doi: 10.1016/j.ceca.2005.06.019 pubmed: 16087231
Verkhratsky, A. Physiology and pathophysiology of the calcium store in the endoplasmic reticulum of neurons. Physiol. Rev. 85, 201–279. https://doi.org/10.1152/physrev.00004.2004 (2005).
doi: 10.1152/physrev.00004.2004 pubmed: 15618481
Xu, C. Y., Bailly-Maitre, B. & Reed, J. C. Endoplasmic reticulum stress: cell life and death decisions. J. Clin. Investig. 115, 2656–2664. https://doi.org/10.1172/jc126373 (2005).
doi: 10.1172/jc126373 pubmed: 16200199
Verkhratsky, A. J. & Petersen, O. H. Neuronal calcium stores. Cell Calcium 24, 333–343. https://doi.org/10.1016/s0143-4160(98)90057-4 (1998).
doi: 10.1016/s0143-4160(98)90057-4 pubmed: 10091003
Pawson, T. Dynamic control of signaling by modular adaptor proteins. Curr. Opin. Cell Biol. 19, 112–116. https://doi.org/10.1016/j.ceb.2007.02.013 (2007).
doi: 10.1016/j.ceb.2007.02.013 pubmed: 17317137
Algenstaedt, P. M., Antonetti, D. A., Yaffe, M. B. & Kahn, C. R. Insulin receptor substrate proteins create a link between the tyrosine phosphorylation cascade and the Ca
doi: 10.1074/jbc.272.38.23696 pubmed: 9295312
Lencesova, L., O’Neill, A., Resneck, W. G., Bloch, R. J. & Blaustein, M. P. Plasma membrane-cytoskeleton-endoplasmic reticulum complexes in neurons and astrocytes. J. Biol. Chem. 279, 2885–2893. https://doi.org/10.1074/jbc.M310365200 (2004).
doi: 10.1074/jbc.M310365200 pubmed: 14593108
Manning, G., Young, S. L., Miller, W. T. & Zhai, Y. The protist, Monosiga brevicollis, has a tyrosine kinase signaling network more elaborate and diverse than found in any known metazoan. Proc. Natl. Acad. Sci. U.S.A. 105, 9674–9679. https://doi.org/10.1073/pnas.0801314105 (2008).
doi: 10.1073/pnas.0801314105 pubmed: 18621719 pmcid: 2453073
Wills, M. K. B. & Jones, N. Teaching an old dogma new tricks: twenty years of Shc adaptor signalling. Biochem. J. 447, 1–16. https://doi.org/10.1042/bj20120769 (2012).
doi: 10.1042/bj20120769 pubmed: 22970934
Kojima, T. et al. Genomic organization of the Shc-related phosphotyrosine adapters and characterization of the full-length Sck/ShcB: Specific association of p68-Sck/ShcB with pp135. Biochem. Biophys. Res. Commun. 284, 1039–1047. https://doi.org/10.1006/bbrc.2001.5080 (2001).
doi: 10.1006/bbrc.2001.5080 pubmed: 11409899
Conti, L. et al. Shc signaling in differentiating neural progenitor cells. Nat. Neurosci. 4, 579–586. https://doi.org/10.1038/88395 (2001).
doi: 10.1038/88395 pubmed: 11369938
Miyamoto, Y. et al. Hippocampal synaptic modulation by the phosphotyrosine adapter protein ShcC/N-Shc via interaction with the NMDA receptor. J. Neurosci. 25, 1826–1835. https://doi.org/10.1523/jneurosci.3030-04.2005 (2005).
doi: 10.1523/jneurosci.3030-04.2005 pubmed: 15716419 pmcid: 6725942
Sakai, R. et al. The mammalian ShcB and ShcC phosphotyrosine docking proteins function in the maturation of sensory and sympathetic neurons. Neuron 28, 819–833. https://doi.org/10.1016/s0896-6273(00)00156-2 (2000).
doi: 10.1016/s0896-6273(00)00156-2 pubmed: 11163269
Conti, L. et al. Expression and activation of SH2/PTB-containing ShcA adaptor protein reflects the pattern of neurogenesis in the mammalian brain. Proc. Natl. Acad. Sci. U.S.A. 94, 8185–8190 (1997).
doi: 10.1073/pnas.94.15.8185
Nakamura, T., Muraoka, S., Sanokawa, R. & Mori, N. N-Shc and Sck, two neuronally expressed Shc adapter homologs—their differential regional expression in the brain and roles in neurotrophin and Src signaling. J. Biol. Chem. 273, 6960–6967. https://doi.org/10.1074/jbc.273.12.6960 (1998).
doi: 10.1074/jbc.273.12.6960 pubmed: 9507002
O’Bryan, J. P., Zhou, S. Y., Cantley, L., Der, C. J. & Pawson, T. A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is specifically expressed in the brain. Proc. Natl. Acad. Sci. U.S.A. 93, 2729–2734. https://doi.org/10.1073/pnas.93.7.2729 (1996).
doi: 10.1073/pnas.93.7.2729 pubmed: 8610109 pmcid: 39699
Nakamura, T. et al. N-Shc: a neural-specific adapter molecule that mediates signaling from neurotrophin/Trk to Ras/MAPK pathway. Oncogene 13, 1111–1121 (1996).
pubmed: 8808684
Robeson, H. N. et al. Localization of phosphotyrosine adaptor protein ShcD/SHC4 in the adult rat central nervous system. BMC Neurosci. 20, 57. https://doi.org/10.1186/s12868-019-0541-5 (2019).
doi: 10.1186/s12868-019-0541-5 pubmed: 31823725 pmcid: 6902498
Lai, K. M. V. & Pawson, T. The ShcA phosphotyrosine docking protein sensitizes cardiovascular signaling in the mouse embryo. Genes Dev. 14, 1132–1145 (2000).
pubmed: 10809671 pmcid: 316585
Cattaneo, E. & Pelicci, P. G. Emerging roles for SH2/PTB-containing Shc adaptor proteins in the developing mammalian brain. Trends Neurosci. 21, 476–481. https://doi.org/10.1016/s0166-2236(98)01282-x (1998).
doi: 10.1016/s0166-2236(98)01282-x pubmed: 9829689
Ravichandran, K. S. Signaling via Shc family adapter proteins. Oncogene 20, 6322–6330. https://doi.org/10.1038/sj.onc.1204776 (2001).
doi: 10.1038/sj.onc.1204776 pubmed: 11607835
Nakamura, T. et al. Discrimination between phosphotyrosine-mediated signaling properties of conventional and neuronal Shc adapter molecules. Oncogene 21, 22–31. https://doi.org/10.1038/sj.onc.1205019 (2002).
doi: 10.1038/sj.onc.1205019 pubmed: 11791173
Ponti, G. et al. Comparative expression profiles of ShcB and ShcC phosphotyrosine adapter molecules in the adult brain. Neuroscience 133, 105–115. https://doi.org/10.1016/j.neuroscience.2005.02.014 (2005).
doi: 10.1016/j.neuroscience.2005.02.014 pubmed: 15893635
McCormick, D. A. & Thompson, R. F. Cerebellum - Essential involvement in the classically-conditioned eyelid response. Science 223, 296–299. https://doi.org/10.1126/science.6701513 (1984).
doi: 10.1126/science.6701513 pubmed: 6701513
Ito, M. The molecular organization of cerebellar long-term depression. Nat. Rev. Neurosci. 3, 896–902. https://doi.org/10.1038/nrn962 (2002).
doi: 10.1038/nrn962 pubmed: 12415297
Linden, D. J. & Connor, J. A. Long-term synaptic depression. Annu. Rev. Neurosci. 18, 319–357. https://doi.org/10.1146/annurev.ne.18.030195.001535 (1995).
doi: 10.1146/annurev.ne.18.030195.001535 pubmed: 7605065
Maejima, T., Hashimoto, K., Yoshida, T., Aiba, A. & Kano, M. Presynaptic inhibition caused by retrograde signal from metabotropic glutamate to cannabinoid receptors. Neuron 31, 463–475. https://doi.org/10.1016/s0896-6273(01)00375-0 (2001).
doi: 10.1016/s0896-6273(01)00375-0 pubmed: 11516402
Bliss, T. V. & Collingridge, G. L. A synaptic model of memory: long-term potentiation in the hippocampus. Nature 361, 31–39. https://doi.org/10.1038/361031a0 (1993).
doi: 10.1038/361031a0 pubmed: 8421494
Finch, E. A. & Augustine, G. J. Local calcium signalling by inositol-1,4, 5-trisphosphate in Purkinje cell dendrites. Nature 396, 753–756 (1998).
doi: 10.1038/25541
Kakizawa, S. et al. Junctophilin-mediated channel crosstalk essential for cerebellar synaptic plasticity. EMBO J. 26, 1924–1933. https://doi.org/10.1038/sj.emboj.7601639 (2007).
doi: 10.1038/sj.emboj.7601639 pubmed: 17347645 pmcid: 1847665
Kakizawa, S. Nitric oxide-induced calcium release: activation of type 1 ryanodine receptor, a calcium release channel, through non-enzymatic post-translational modification by nitric oxide. Front. Endocrinol. 4, 142. https://doi.org/10.3389/fendo.2013.00142 (2013).
doi: 10.3389/fendo.2013.00142
Kakizawa, S. et al. Nitric oxide-induced calcium release via ryanodine receptors regulates neuronal function. EMBO J. 31, 417–428. https://doi.org/10.1038/emboj.2011.386 (2012).
doi: 10.1038/emboj.2011.386 pubmed: 22036948
Mikami, Y. et al. Nitric oxide-induced activation of the type 1 ryanodine receptor is critical for epileptic seizure-induced neuronal cell death. EBioMedicine 11, 253–261. https://doi.org/10.1016/j.ebiom.2016.08.020 (2016).
doi: 10.1016/j.ebiom.2016.08.020 pubmed: 27544065 pmcid: 5049986
Mori, F., Fukaya, M., Abe, H., Wakabayashi, K. & Watanabe, M. Developmental changes in expression of the three ryanodine receptor mRNAs in the mouse brain. Neurosci. Lett. 285, 57–60. https://doi.org/10.1016/s0304-3940(00)01046-6 (2000).
doi: 10.1016/s0304-3940(00)01046-6 pubmed: 10788707
Wojcikiewicz, R. J. H. Tipe-I, type-II, and type-III inositol 1,4,5-trisphosphate receptors are unequally susceptible to down-regulation and are expressed in markedly different proportions in different cell-types. J. Biol. Chem. 270, 11678–11683. https://doi.org/10.1074/jbc.270.19.11678 (1995).
doi: 10.1074/jbc.270.19.11678 pubmed: 7744807
Usachev, Y. M., Marsh, A. J., Johanns, T. M., Lemke, M. M. & Thayer, S. A. Activation of protein kinase C in sensory neurons accelerates Ca
doi: 10.1523/jneurosci.2920-05.2006 pubmed: 16399701 pmcid: 6674318
Brini, M. & Carafoli, E. Calcium pumps in health and disease. Physiol. Rev. 89, 1341–1378. https://doi.org/10.1152/physrev.00032.2008 (2009).
doi: 10.1152/physrev.00032.2008 pubmed: 19789383
Mata, A. M. & Sepulveda, M. R. Calcium pumps in the central nervous system. Brain Res. Rev. 49, 398–405. https://doi.org/10.1016/j.brainresrev.2004.11.004 (2005).
doi: 10.1016/j.brainresrev.2004.11.004 pubmed: 16111566
Bhupathy, P., Babu, G. J. & Periasamy, M. Sarcolipin and phospholamban as regulators of cardiac sarcoplasmic reticulum Ca
doi: 10.1016/j.yjmcc.2007.03.738 pubmed: 17442337 pmcid: 2743185
Stammers, A. N. et al. The regulation of sarco(endo)plasmic reticulum calcium-ATPases (SERCA). Can. J. Physiol. Pharmacol. 93, 843–854. https://doi.org/10.1139/cjpp-2014-0463 (2015).
doi: 10.1139/cjpp-2014-0463 pubmed: 25730320
MacLennan, D. H. & Kranias, E. G. Phospholamban: a crucial regulator of cardiac contractility. Nat. Rev. Mol. Cell Biol. 4, 566–577. https://doi.org/10.1038/nrm1151 (2003).
doi: 10.1038/nrm1151 pubmed: 12838339
Asahi, M. et al. Sarcolipin regulates sarco(endo)plasmic reticulum Ca
doi: 10.1073/pnas.0330962100 pubmed: 12692302 pmcid: 154294
Vangheluwe, P., Raeymaekers, L., Dode, L. & Wuytack, F. Modulating sarco(endo)plasmic reticulum Ca(2+) ATPase 2 (SERCA2) activity: cell biological implications. Cell Calcium 38, 291–302. https://doi.org/10.1016/j.ceca.2005.06.033 (2005).
doi: 10.1016/j.ceca.2005.06.033 pubmed: 16105684
Christian, K. M. & Thompson, R. F. Neural substrates of eyeblink conditioning: acquisition and retention. Learn. Mem. 10, 427–455. https://doi.org/10.1101/lm.59603 (2003).
doi: 10.1101/lm.59603 pubmed: 14657256
Ito, M. Cerebellar long-term depression: characterization, signal transduction, and functional roles. Physiol. Rev. 81, 1143–1195 (2001).
doi: 10.1152/physrev.2001.81.3.1143
Kakizawa, S. et al. Maintenance of presynaptic function by AMPA receptor-mediated excitatory postsynaptic activity in adult brain. Proc. Natl. Acad. Sci. U.S.A. 102, 19180–19185. https://doi.org/10.1073/pnas.0504359103 (2005).
doi: 10.1073/pnas.0504359103 pubmed: 16357208 pmcid: 1323150
Kakizawa, S., Yamasaki, M., Watanabe, M. & Kano, M. Critical period for activity-dependent synapse elimination in developing cerebellum. J. Neurosci. 20, 4954–4961 (2000).
doi: 10.1523/JNEUROSCI.20-13-04954.2000
Kishimoto, Y. et al. mGluR1 in cerebellar Purkinje cells is required for normal association of temporally contiguous stimuli in classical conditioning. Eur. J. Neurosci. 16, 2416–2424. https://doi.org/10.1046/j.1460-9568.2002.02407.x (2002).
doi: 10.1046/j.1460-9568.2002.02407.x pubmed: 12492436
Kishimoto, Y. et al. Age-dependent impairment of eyeblink conditioning in prion protein-deficient mice. PLoS ONE 8, e60627. https://doi.org/10.1371/journal.pone.0060627 (2013).
doi: 10.1371/journal.pone.0060627 pubmed: 23593266 pmcid: 3622692
Anderson, K. D., Abdul, M. & Steward, O. Quantitative assessment of deficits and recovery of forelimb motor function after cervical spinal cord injury in mice. Exp. Neurol. 190, 184–191. https://doi.org/10.1016/j.expneurol.2004.06.029 (2004).
doi: 10.1016/j.expneurol.2004.06.029 pubmed: 15473991
Susick, L. L. et al. Adenylyl cylases 1 and 8 mediate select striatal-dependent behaviors and sensitivity to ethanol stimulation in the adolescent period following acute neonatal ethanol exposure. Behav. Brain Res. 269, 66–74. https://doi.org/10.1016/j.bbr.2014.04.031 (2014).
doi: 10.1016/j.bbr.2014.04.031 pubmed: 24769171 pmcid: 4074522
Miyamoto, Y. et al. Lower sensitivity to stress and altered monoaminergic neuronal function in mice lacking the NMDA receptor epsilon 4 subunit. J. Neurosci. 22, 2335–2342 (2002).
doi: 10.1523/JNEUROSCI.22-06-02335.2002
Noda, Y., Yamada, K., Furukawa, H. & Nabeshima, T. Enhancement of immobility in a forced swimming test by subacute or repeated treatment with phencyclidine: a new model of schizophrenia. Br. J. Pharmacol. 116, 2531–2537. https://doi.org/10.1111/j.1476-5381.1995.tb15106.x (1995).
doi: 10.1111/j.1476-5381.1995.tb15106.x pubmed: 8581295 pmcid: 1909055
Edwards, F. A., Konnerth, A., Sakmann, B. & Takahashi, T. A thin slice preparation for patch clamps recordings from neurons of the mammalian central nervous-system. Pflugers Arch. 414, 600–612. https://doi.org/10.1007/bf00580998 (1989).
doi: 10.1007/bf00580998 pubmed: 2780225
Namiki, S., Kakizawa, S., Hirose, K. & Iino, M. NO signalling decodes frequency of neuronal activity and generates synapse-specific plasticity in mouse cerebellum. J. Physiol. (Lond.) 566, 849–863. https://doi.org/10.1113/jphysiol.2005.088799 (2005).
doi: 10.1113/jphysiol.2005.088799

Auteurs

Sho Kakizawa (S)

Department of Anatomy and Neurobiology, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, 852-8523, Japan. kakizawa.sho.4u@kyoto-u.ac.jp.
Department of Biological Chemistry, Graduate School of Pharmaceutical Science, Kyoto University, Sakyo-ku, Kyoto, 606-8501, Japan. kakizawa.sho.4u@kyoto-u.ac.jp.

Yasushi Kishimoto (Y)

Department of Biophysics, Kagawa School of Pharmaceutical Sciences, Tokushima Bunri University, Sanuki, Kagawa, 769-2193, Japan.

Shinichiro Yamamoto (S)

Department of Biological Chemistry, Graduate School of Pharmaceutical Science, Kyoto University, Sakyo-ku, Kyoto, 606-8501, Japan.
Division of Pharmacology, Faculty of Pharmaceutical Sciences, Teikyo Heisei University, Nakano-ku, Tokyo, 164-8530, Japan.

Kazuko Onga (K)

Department of Anatomy and Neurobiology, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, 852-8523, Japan.

Kunihiko Yasuda (K)

Department of Anatomy and Neurobiology, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, 852-8523, Japan.
Department of Occupational Therapy, Faculty of Fukuoka Medical Technology, Teikyo University, Omuta, 836-8505, Japan.

Yoshiaki Miyamoto (Y)

Department of Pharmaceutical Therapy and Neuropharmacology, Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama, 930-0194, Japan.

Masahiko Watanabe (M)

Department of Anatomy, Hokkaido University School of Medicine, Sapporo, 060-8638, Japan.

Ryuichi Sakai (R)

Department of Biochemistry, Kitasato University School of Medicine, Sagamihara, Kanagawa, 252-0373, Japan.

Nozomu Mori (N)

Department of Anatomy and Neurobiology, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, 852-8523, Japan. morinosm@takagigakuen.ac.jp.
Faculty of Medicine, Fukuoka International University of Health and Welfare, Fukuoka, 814-0001, Japan. morinosm@takagigakuen.ac.jp.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female

Evaluation of Low-Value Services Across Major Medicare Advantage Insurers and Traditional Medicare.

Ciara Duggan, Adam L Beckman, Ishani Ganguli et al.
1.00
Humans United States Aged Cross-Sectional Studies Medicare Part C

Effectiveness of Virtual Yoga for Chronic Low Back Pain: A Randomized Clinical Trial.

Hallie Tankha, Devyn Gaskins, Amanda Shallcross et al.
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › Functional maintenance of calcium store by...
questionsmedicales.fr › Facteurs biologiques › Facteurs de la coagulation sanguine › Calcium › Functional maintenance of calcium store by...
questionsmedicales.fr › Phénomènes physiologiques cellulaires › Transduction du signal › Systèmes de seconds messagers › Signalisation calcique › Functional maintenance of calcium store by...
questionsmedicales.fr › Système nerveux › Système nerveux central › Encéphale › Tronc cérébral › Rhombencéphale › Métencéphale › Cervelet › Functional maintenance of calcium store by...
questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Organites › Réticulum endoplasmique › Functional maintenance of calcium store by...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Functional maintenance of calcium store by...
questionsmedicales.fr › Phénomènes physiologiques de l'appareil locomoteur et du système nerveux › Phénomènes physiologiques du système nerveux › Plasticité neuronale › Dépression synaptique à long terme › Functional maintenance of calcium store by...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Functional maintenance of calcium store by...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Souris transgéniques › Souris knockout › Functional maintenance of calcium store by...
questionsmedicales.fr › Troubles mentaux › Troubles moteurs › Functional maintenance of calcium store by...
questionsmedicales.fr › Phénomènes physiologiques de l'appareil locomoteur et du système nerveux › Phénomènes physiologiques du système nerveux › Plasticité neuronale › Functional maintenance of calcium store by...
questionsmedicales.fr › Cellules › Neurones › Cellules de Purkinje › Functional maintenance of calcium store by...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Protéines de transport membranaire › P-type ATPases › Calcium-Transporting ATPases › Sarcoplasmic Reticulum Calcium-Transporting ATPases › Functional maintenance of calcium store by...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protéines adaptatrices de la transduction du signal › Protéines adaptatrices de signalisation Shc › Protéine transformante-2 contenant un domaine d'homologie-2 de Src › Functional maintenance of calcium store by...
questionsmedicales.fr › Cellules › Structures cellulaires › Membrane cellulaire › Structures de la membrane cellulaire › Jonctions intercellulaires › Synapses › Functional maintenance of calcium store by...