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dc.contributor.authorDobbins, G Clement
dc.contributor.authorLuo, Shiwen
dc.contributor.authorYang, Zhihua
dc.contributor.authorXiong, Wen C
dc.contributor.authorMei, Lin
dc.date.accessioned2010-09-24T21:26:49Z
dc.date.available2010-09-24T21:26:49Z
dc.date.issued2009-01-13en_US
dc.identifier.citationMol Brain. 2008 Dec 3; 1:18en_US
dc.identifier.issn1756-6606en_US
dc.identifier.pmid19055765en_US
dc.identifier.doi10.1186/1756-6606-1-18en_US
dc.identifier.urihttp://hdl.handle.net/10675.2/59
dc.description.abstract: AChR is concentrated at the postjunctional membrane at the neuromuscular junction. However, the underlying mechanism is unclear. We show that alpha-actinin, a protein known to cross-link F-actin, interacts with rapsyn, a scaffold protein essential for neuromuscular junction formation. alpha-Actinin, rapsyn, and surface AChR form a ternary complex. Moreover, the rapsyn-alpha-actinin interaction is increased by agrin, a factor known to stimulate AChR clustering. Downregulation of alpha-actinin expression inhibits agrin-mediated AChR clustering. Furthermore, the rapsyn-alpha-actinin interaction can be disrupted by inhibiting Abl and by cholinergic stimulation. Together these results indicate a role for alpha-actinin in AChR clustering.
dc.rightsThe PMC Open Access Subset is a relatively small part of the total collection of articles in PMC. Articles in the PMC Open Access Subset are still protected by copyright, but are made available under a Creative Commons or similar license that generally allows more liberal redistribution and reuse than a traditional copyrighted work. Please refer to the license statement in each article for specific terms of use. The license terms are not identical for all articles in this subset.en_US
dc.titlealpha-Actinin interacts with rapsyn in agrin-stimulated AChR clustering.en_US
dc.typeJournal Articleen_US
dc.identifier.pmcidPMC2621155en_US
dc.contributor.corporatenameInstitute of Molecular Medicine and Geneticsen_US
dc.contributor.corporatenameDepartment of Neuroscience and Regenerative Medicineen_US
refterms.dateFOA2019-04-09T22:04:10Z
html.description.abstract: AChR is concentrated at the postjunctional membrane at the neuromuscular junction. However, the underlying mechanism is unclear. We show that alpha-actinin, a protein known to cross-link F-actin, interacts with rapsyn, a scaffold protein essential for neuromuscular junction formation. alpha-Actinin, rapsyn, and surface AChR form a ternary complex. Moreover, the rapsyn-alpha-actinin interaction is increased by agrin, a factor known to stimulate AChR clustering. Downregulation of alpha-actinin expression inhibits agrin-mediated AChR clustering. Furthermore, the rapsyn-alpha-actinin interaction can be disrupted by inhibiting Abl and by cholinergic stimulation. Together these results indicate a role for alpha-actinin in AChR clustering.


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