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Article: Akt phosphorylation of zyxin mediates its interaction with acinus-S and prevents acinus-triggered chromatin condensation

TitleAkt phosphorylation of zyxin mediates its interaction with acinus-S and prevents acinus-triggered chromatin condensation
Authors
Issue Date2007
Citation
Cell Death and Differentiation, 2007, v. 14, n. 9, p. 1688-1699 How to Cite?
AbstractZyxin, a focal adhesion molecule, contains LIM domains and shuttles between the cytoplasm and the nucleus. Nuclear zyxin promotes cardiomyocyte survival, which is mediated by nuclear-activated Akt. However, the molecular mechanism of how zyxin antagonizes apoptosis remains elusive. Here, we report that zyxin binds to acinus-S, a nuclear speckle protein inducing apoptotic chromatin condensation after cleavage by caspases, and prevents its apoptotic action, which is regulated by Akt. Akt binds and phosphorylates zyxin on serine 142, leading to its association with acinus. Interestingly, 14-3-3γ, but not ζ isoform selectively, triggers zyxin nuclear translocation, which is Akt phosphorylation dependent. Zyxin is also a substrate of caspases, but Akt phosphorylation is unable to prevent its apoptotic cleavage. Expression of zyxin S142D, a phosphorylation mimetic mutant, diminishes acinus proteolytic cleavage and chromatin condensation; by contrast, wild-type zyxin or unphosphorylated S142A mutant fails. Thus, Akt regulates zyxin/acinus complex formation in the nucleus, contributing to suppression of apoptosis.
Persistent Identifierhttp://hdl.handle.net/10722/225044
ISSN
2015 Impact Factor: 8.218
2015 SCImago Journal Rankings: 4.219

 

DC FieldValueLanguage
dc.contributor.authorChan, C. B.-
dc.contributor.authorLiu, X.-
dc.contributor.authorTang, X.-
dc.contributor.authorFu, H.-
dc.contributor.authorYe, K.-
dc.date.accessioned2016-04-18T11:16:36Z-
dc.date.available2016-04-18T11:16:36Z-
dc.date.issued2007-
dc.identifier.citationCell Death and Differentiation, 2007, v. 14, n. 9, p. 1688-1699-
dc.identifier.issn1350-9047-
dc.identifier.urihttp://hdl.handle.net/10722/225044-
dc.description.abstractZyxin, a focal adhesion molecule, contains LIM domains and shuttles between the cytoplasm and the nucleus. Nuclear zyxin promotes cardiomyocyte survival, which is mediated by nuclear-activated Akt. However, the molecular mechanism of how zyxin antagonizes apoptosis remains elusive. Here, we report that zyxin binds to acinus-S, a nuclear speckle protein inducing apoptotic chromatin condensation after cleavage by caspases, and prevents its apoptotic action, which is regulated by Akt. Akt binds and phosphorylates zyxin on serine 142, leading to its association with acinus. Interestingly, 14-3-3γ, but not ζ isoform selectively, triggers zyxin nuclear translocation, which is Akt phosphorylation dependent. Zyxin is also a substrate of caspases, but Akt phosphorylation is unable to prevent its apoptotic cleavage. Expression of zyxin S142D, a phosphorylation mimetic mutant, diminishes acinus proteolytic cleavage and chromatin condensation; by contrast, wild-type zyxin or unphosphorylated S142A mutant fails. Thus, Akt regulates zyxin/acinus complex formation in the nucleus, contributing to suppression of apoptosis.-
dc.languageeng-
dc.relation.ispartofCell Death and Differentiation-
dc.titleAkt phosphorylation of zyxin mediates its interaction with acinus-S and prevents acinus-triggered chromatin condensation-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1038/sj.cdd.4402179-
dc.identifier.pmid17572661-
dc.identifier.scopuseid_2-s2.0-34548015212-
dc.identifier.volume14-
dc.identifier.issue9-
dc.identifier.spage1688-
dc.identifier.epage1699-
dc.identifier.eissn1476-5403-

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