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Article: α-syntrophin regulates ARMS localization at the neuromuscular junction and enhances EphA4 signaling in an ARMS-dependent manner

Titleα-syntrophin regulates ARMS localization at the neuromuscular junction and enhances EphA4 signaling in an ARMS-dependent manner
Authors
Issue Date2005
Citation
Journal of Cell Biology, 2005, v. 169 n. 5, p. 813-824 How to Cite?
AbstractEphA4 signaling has recently been implicated in the regulation of synapse formation and plasticity. In this study, we show that ankyrin repeat-rich membrane spanning (ARMS; also known as a kinase D-interacting substrate of 220 kD), a substrate for ephrin and neurotrophin receptors, was expressed in developing muscle and was concentrated at the neuromuscular junction (NMJ). Using yeast two-hybrid screening, we identified a PDZ (PSD-95, Dlg, ZO-1) domain protein, α-syntrophin, as an ARMS-interacting protein in muscle. Overexpression of α-syntrophin induced ARMS clustering in a PDZ domain-dependent manner. Coexpression of ARMS enhanced EphA4 signaling, which was further augmented by the presence of α-syntrophin. Moreover, the ephrin-A1-induced tyrosine phosphorylation of EphA4 was reduced in C2C12 myotubes after the blockade of ARMS and α-syntrophin expression by RNA interference. Finally, α-syntrophin-null mice exhibited a disrupted localization of ARMS and EphA4 at the NMJ and a reduced expression of ARMS in muscle. Altogether, our findings suggest that ARMS may play an important role in regulating postsynaptic signal transduction through the syntrophin-mediated localization of receptor tyrosine kinases such as EphA4. © The Rockefeller University Press.
Persistent Identifierhttp://hdl.handle.net/10722/196661
ISSN
2015 Impact Factor: 8.717
2015 SCImago Journal Rankings: 7.923
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLuo, S-
dc.contributor.authorChen, Y-
dc.contributor.authorLai, K-O-
dc.contributor.authorArévalo, JC-
dc.contributor.authorFroehner, SC-
dc.contributor.authorAdams, ME-
dc.contributor.authorChao, MV-
dc.contributor.authorIp, NY-
dc.date.accessioned2014-04-24T02:10:31Z-
dc.date.available2014-04-24T02:10:31Z-
dc.date.issued2005-
dc.identifier.citationJournal of Cell Biology, 2005, v. 169 n. 5, p. 813-824-
dc.identifier.issn0021-9525-
dc.identifier.urihttp://hdl.handle.net/10722/196661-
dc.description.abstractEphA4 signaling has recently been implicated in the regulation of synapse formation and plasticity. In this study, we show that ankyrin repeat-rich membrane spanning (ARMS; also known as a kinase D-interacting substrate of 220 kD), a substrate for ephrin and neurotrophin receptors, was expressed in developing muscle and was concentrated at the neuromuscular junction (NMJ). Using yeast two-hybrid screening, we identified a PDZ (PSD-95, Dlg, ZO-1) domain protein, α-syntrophin, as an ARMS-interacting protein in muscle. Overexpression of α-syntrophin induced ARMS clustering in a PDZ domain-dependent manner. Coexpression of ARMS enhanced EphA4 signaling, which was further augmented by the presence of α-syntrophin. Moreover, the ephrin-A1-induced tyrosine phosphorylation of EphA4 was reduced in C2C12 myotubes after the blockade of ARMS and α-syntrophin expression by RNA interference. Finally, α-syntrophin-null mice exhibited a disrupted localization of ARMS and EphA4 at the NMJ and a reduced expression of ARMS in muscle. Altogether, our findings suggest that ARMS may play an important role in regulating postsynaptic signal transduction through the syntrophin-mediated localization of receptor tyrosine kinases such as EphA4. © The Rockefeller University Press.-
dc.languageeng-
dc.relation.ispartofJournal of Cell Biology-
dc.titleα-syntrophin regulates ARMS localization at the neuromuscular junction and enhances EphA4 signaling in an ARMS-dependent manner-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1083/jcb.200412008-
dc.identifier.pmid15939763-
dc.identifier.scopuseid_2-s2.0-22344445407-
dc.identifier.volume169-
dc.identifier.issue5-
dc.identifier.spage813-
dc.identifier.epage824-
dc.identifier.isiWOS:000229600100015-

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