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Article: SRPK2 phosphorylates tau and mediates the cognitive defects in Alzheimer's disease

TitleSRPK2 phosphorylates tau and mediates the cognitive defects in Alzheimer's disease
Authors
Issue Date2012
Citation
Journal of Neuroscience, 2012, v. 32, n. 48, p. 17262-17272 How to Cite?
AbstractSerine-arginine protein kinases 2 (SRPK2) is a cell cycle-regulated kinase that phosphorylates serine/arginine domain-containing proteins and mediates pre-mRNA splicing with unclear function in neurons. Here, we show that SRPK2 phosphorylates tau on S214, suppresses tau-dependent microtubule polymerization, and inhibits axonal elongationin neurons. DepletionofSRPK2in dentate gyrus inhibits tau phosphorylation in APP/PS1 mouse and alleviates the impaired cognitive behaviors. The defective LTP in APP/PS1 mice is also improved after SRPK2 depletion. Moreover, active SRPK2isincreasedinthe cortexof APP/PS1 mice and the pathological structures of human Alzheimer's disease (AD) brain. Therefore, our study suggestsSRPK2may contributetothe formationofhyperphosphorylated tau and the pathogenesis of AD. © 2012 the authors.
Persistent Identifierhttp://hdl.handle.net/10722/225043
ISSN
2015 Impact Factor: 5.924
2015 SCImago Journal Rankings: 5.105

 

DC FieldValueLanguage
dc.contributor.authorHong, Yi-
dc.contributor.authorChan, Chi Bun-
dc.contributor.authorKwon, Il Sun-
dc.contributor.authorLi, Xuekun-
dc.contributor.authorSong, Mingke-
dc.contributor.authorLee, Hyun Pil-
dc.contributor.authorLiu, Xia-
dc.contributor.authorSompol, Pradoldej-
dc.contributor.authorJin, Peng-
dc.contributor.authorLee, Hyoung Gon-
dc.contributor.authorYu, Shan Ping-
dc.contributor.authorYe, Keqiang-
dc.date.accessioned2016-04-18T11:16:36Z-
dc.date.available2016-04-18T11:16:36Z-
dc.date.issued2012-
dc.identifier.citationJournal of Neuroscience, 2012, v. 32, n. 48, p. 17262-17272-
dc.identifier.issn0270-6474-
dc.identifier.urihttp://hdl.handle.net/10722/225043-
dc.description.abstractSerine-arginine protein kinases 2 (SRPK2) is a cell cycle-regulated kinase that phosphorylates serine/arginine domain-containing proteins and mediates pre-mRNA splicing with unclear function in neurons. Here, we show that SRPK2 phosphorylates tau on S214, suppresses tau-dependent microtubule polymerization, and inhibits axonal elongationin neurons. DepletionofSRPK2in dentate gyrus inhibits tau phosphorylation in APP/PS1 mouse and alleviates the impaired cognitive behaviors. The defective LTP in APP/PS1 mice is also improved after SRPK2 depletion. Moreover, active SRPK2isincreasedinthe cortexof APP/PS1 mice and the pathological structures of human Alzheimer's disease (AD) brain. Therefore, our study suggestsSRPK2may contributetothe formationofhyperphosphorylated tau and the pathogenesis of AD. © 2012 the authors.-
dc.languageeng-
dc.relation.ispartofJournal of Neuroscience-
dc.titleSRPK2 phosphorylates tau and mediates the cognitive defects in Alzheimer's disease-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1523/JNEUROSCI.3300-12.2012-
dc.identifier.pmid23197718-
dc.identifier.scopuseid_2-s2.0-84870228676-
dc.identifier.volume32-
dc.identifier.issue48-
dc.identifier.spage17262-
dc.identifier.epage17272-
dc.identifier.eissn1529-2401-

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