Please use this identifier to cite or link to this item: https://doi.org/10.1523/JNEUROSCI.4181-06.2007
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dc.titleSirtuin 2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating α-tubulin
dc.contributor.authorLi, W.
dc.contributor.authorZhang, B.
dc.contributor.authorTang, J.
dc.contributor.authorCao, Q.
dc.contributor.authorWu, Y.
dc.contributor.authorWu, C.
dc.contributor.authorGuo, J.
dc.contributor.authorLing, E.-A.
dc.contributor.authorLiang, F.
dc.date.accessioned2011-07-18T08:45:24Z
dc.date.available2011-07-18T08:45:24Z
dc.date.issued2007
dc.identifier.citationLi, W., Zhang, B., Tang, J., Cao, Q., Wu, Y., Wu, C., Guo, J., Ling, E.-A., Liang, F. (2007). Sirtuin 2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating α-tubulin. Journal of Neuroscience 27 (10) : 2606-2616. ScholarBank@NUS Repository. https://doi.org/10.1523/JNEUROSCI.4181-06.2007
dc.identifier.issn02706474
dc.identifier.issn02706474
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/23968
dc.description.abstractSilent information regulator-2 (SIR2) proteins regulate lifespan of diverse organisms, but their distribution and roles in the CNS remain unclear. Here,we show that sirtuin 2 (SIRT2), a mammalian SIR2 homolog, is an oligodendroglial cytoplasmic protein and localized to the outer and juxtanodal loops in the myelin sheath. Among cytoplasmic proteins of OLN-93 oligodendrocytes, ?-tubulin was the main substrate of SIRT2 deacetylase. In cultured primary oligodendrocyte precursors (OLPs), SIRT2 emergence accompanied elevated ?-tubulin acetylation and OLP differentiation into the prematurity stage. Small interfering RNA knockdown of SIRT2 increased the ?-tubulin acetylation, myelin basic protein expression, and cell arbor complexity of OLPs. SIRT2 overexpression had the opposite effects, and counteracted the cell arborization-promoting effect of overexpressed juxtanodin. SIRT2 mutation concomitantly reduced its deacetylase activity and its impeding effect on OLP arborization. These results demonstrated a counterbalancing role of SIRT2 against a facilitatory effect of tubulin acetylation on oligodendroglial differentiation. Selective SIRT2 availability to oligodendroglia may have important implications for myelinogenesis, myelin-axon interaction, and brain aging. Copyright � 2007 Society for Neuroscience.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1523/JNEUROSCI.4181-06.2007
dc.publisherSociety for Neuroscience
dc.sourceScopus
dc.subjectCytoskeleton
dc.subjectMyelination
dc.subjectOligodendrocyte differentiation
dc.subjectRNA interference
dc.subjectSirtuin 2
dc.subjectTubulin acetylation/deacetylation
dc.typeArticle
dc.contributor.departmentDEPT OF ANATOMY
dc.description.doi10.1523/JNEUROSCI.4181-06.2007
dc.description.sourcetitleJournal of Neuroscience
dc.description.volume27
dc.description.issue10
dc.description.page2606-2616
dc.identifier.isiut000244758900019
dc.published.statePublished
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