Microtubule-associated protein tau is essential for long-term depression in the hippocampus

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dc.contributor.authorKimura, Tetsuyako
dc.contributor.authorWhitcomb, Daniel J.ko
dc.contributor.authorJo, Jihoonko
dc.contributor.authorRegan, Philipko
dc.contributor.authorPiers, Thomasko
dc.contributor.authorHeo, Seonghooko
dc.contributor.authorBrown, Christopherko
dc.contributor.authorHashikawa, Tsutomuko
dc.contributor.authorMurayama, Miyukiko
dc.contributor.authorSeok, Heonko
dc.contributor.authorSotiropoulos, Ioannisko
dc.contributor.authorKim, Eunjoonko
dc.contributor.authorCollingridge, Graham L.ko
dc.contributor.authorTakashima, Akihikoko
dc.contributor.authorCho, Kwangwookko
dc.date.accessioned2014-09-04T08:30:18Z-
dc.date.available2014-09-04T08:30:18Z-
dc.date.created2014-04-14-
dc.date.created2014-04-14-
dc.date.issued2014-01-
dc.identifier.citationPHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES, v.369, no.1633-
dc.identifier.issn0962-8436-
dc.identifier.urihttp://hdl.handle.net/10203/190013-
dc.description.abstractThe microtubule-associated protein tau is a principal component of neurofibrillary tangles, and has been identified as a key molecule in Alzheimer's disease and other tauopathies. However, it is unknown how a protein that is primarily located in axons is involved in a disease that is believed to have a synaptic origin. To investigate a possible synaptic function of tau, we studied synaptic plasticity in the hippocampus and found a selective deficit in long-term depression (LTD) in tau knockout mice in vivo and in vitro, an effect that was replicated by RNAi knockdown of tau in vitro. We found that the induction of LTD is associated with the glycogen synthase kinase-3-mediated phosphorylation of tau. These observations demonstrate that tau has a critical physiological function in LTD.-
dc.languageEnglish-
dc.publisherROYAL SOC-
dc.subjectGLYCOGEN-SYNTHASE KINASE-3-BETA-
dc.subjectDISEASE-LIKE PHOSPHORYLATION-
dc.subjectPAIRED HELICAL FILAMENT-
dc.subjectALZHEIMERS-DISEASE-
dc.subjectENDOGENOUS TAU-
dc.subjectLOCALIZATION-
dc.subjectPOTENTIATION-
dc.subjectOLIGOMERS-
dc.subjectBINDING-
dc.subjectAGGREGATION-
dc.titleMicrotubule-associated protein tau is essential for long-term depression in the hippocampus-
dc.typeArticle-
dc.identifier.wosid000332463400014-
dc.identifier.scopusid2-s2.0-84888793501-
dc.type.rimsART-
dc.citation.volume369-
dc.citation.issue1633-
dc.citation.publicationnamePHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES-
dc.identifier.doi10.1098/rstb.2013.0144-
dc.embargo.liftdate9999-12-31-
dc.embargo.terms9999-12-31-
dc.contributor.localauthorKim, Eunjoon-
dc.contributor.nonIdAuthorKimura, Tetsuya-
dc.contributor.nonIdAuthorWhitcomb, Daniel J.-
dc.contributor.nonIdAuthorJo, Jihoon-
dc.contributor.nonIdAuthorRegan, Philip-
dc.contributor.nonIdAuthorPiers, Thomas-
dc.contributor.nonIdAuthorHeo, Seonghoo-
dc.contributor.nonIdAuthorBrown, Christopher-
dc.contributor.nonIdAuthorHashikawa, Tsutomu-
dc.contributor.nonIdAuthorMurayama, Miyuki-
dc.contributor.nonIdAuthorSeok, Heon-
dc.contributor.nonIdAuthorSotiropoulos, Ioannis-
dc.contributor.nonIdAuthorCollingridge, Graham L.-
dc.contributor.nonIdAuthorTakashima, Akihiko-
dc.contributor.nonIdAuthorCho, Kwangwook-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorAlzheimer&apos-
dc.subject.keywordAuthors disease-
dc.subject.keywordAuthorhippocampus-
dc.subject.keywordAuthorsynaptic plasticity-
dc.subject.keywordAuthorlong-term depression-
dc.subject.keywordAuthortau-
dc.subject.keywordPlusGLYCOGEN-SYNTHASE KINASE-3-BETA-
dc.subject.keywordPlusDISEASE-LIKE PHOSPHORYLATION-
dc.subject.keywordPlusPAIRED HELICAL FILAMENT-
dc.subject.keywordPlusALZHEIMERS-DISEASE-
dc.subject.keywordPlusENDOGENOUS TAU-
dc.subject.keywordPlusLOCALIZATION-
dc.subject.keywordPlusPOTENTIATION-
dc.subject.keywordPlusOLIGOMERS-
dc.subject.keywordPlusBINDING-
dc.subject.keywordPlusAGGREGATION-
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