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  Role of myosin Va in the plasticity of the vertebrate neuromuscular junction in vivo

Röder, I. V., Petersen, Y., Choi, K. R., Witzemann, V., Hammer, III, J. A., & Rudolf, R. (2008). Role of myosin Va in the plasticity of the vertebrate neuromuscular junction in vivo. PLoS One, 3(12): e3871, pp. 1-16. doi:10.1371/journal.pone.0003871.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-091F-F Version Permalink: http://hdl.handle.net/21.11116/0000-0000-DE31-F
Genre: Journal Article

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Röder, Ira Verena, Author
Petersen, Yvonne, Author
Choi, Kyeong Rok, Author
Witzemann, Veit1, 2, Author              
Hammer, III, John A., Author
Rudolf, Rüdiger, Author
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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 Abstract: BACKGROUND: Myosin Va is a motor protein involved in vesicular transport and its absence leads to movement disorders in humans (Griscelli and Elejalde syndromes) and rodents (e.g. dilute lethal phenotype in mice). We examined the role of myosin Va in the postsynaptic plasticity of the vertebrate neuromuscular junction (NMJ). METHODOLOGY/PRINCIPAL FINDINGS: Dilute lethal mice showed a good correlation between the propensity for seizures, and fragmentation and size reduction of NMJs. In an aneural C2C12 myoblast cell culture, expression of a dominant-negative fragment of myosin Va led to the accumulation of punctate structures containing the NMJ marker protein, rapsyn-GFP, in perinuclear clusters. In mouse hindlimb muscle, endogenous myosin Va co-precipitated with surface-exposed or internalised acetylcholine receptors and was markedly enriched in close proximity to the NMJ upon immunofluorescence. In vivo microscopy of exogenous full length myosin Va as well as a cargo-binding fragment of myosin Va showed localisation to the NMJ in wildtype mouse muscles. Furthermore, local interference with myosin Va function in live wildtype mouse muscles led to fragmentation and size reduction of NMJs, exclusion of rapsyn-GFP from NMJs, reduced persistence of acetylcholine receptors in NMJs and an increased amount of punctate structures bearing internalised NMJ proteins. CONCLUSIONS/SIGNIFICANCE: In summary, our data show a crucial role of myosin Va for the plasticity of live vertebrate neuromuscular junctions and suggest its involvement in the recycling of internalised acetylcholine receptors back to the postsynaptic membrane.

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Language(s): eng - English
 Dates: 2008-07-212008-11-102008-12-052008-12-05
 Publication Status: Published in print
 Pages: 16
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 Rev. Type: Peer
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Title: PLoS One
Source Genre: Journal
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Publ. Info: San Francisco, CA : Public Library of Science
Pages: - Volume / Issue: 3 (12) Sequence Number: e3871 Start / End Page: 1 - 16 Identifier: ISSN: 1932-6203
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000277850