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dc.contributor.authorPandithage, R
dc.contributor.authorLilischkis, R
dc.contributor.authorHarting, K
dc.contributor.authorWolf, A
dc.contributor.authorJedamzik, B
dc.contributor.authorLüscher-Firzlaff, J
dc.contributor.authorVervoorts, J
dc.contributor.authorLasonder, Edwin
dc.contributor.authorKremmer, E
dc.contributor.authorKnöll, B
dc.contributor.authorLüscher, B
dc.date.accessioned2016-07-11T15:04:12Z
dc.date.available2016-07-11T15:04:12Z
dc.date.issued2008-03-10
dc.identifier.issn0021-9525
dc.identifier.issn1540-8140
dc.identifier.urihttp://hdl.handle.net/10026.1/5043
dc.description.abstract

<jats:p>Cyclin-dependent kinases (Cdks) fulfill key functions in many cellular processes, including cell cycle progression and cytoskeletal dynamics. A limited number of Cdk substrates have been identified with few demonstrated to be regulated by Cdk-dependent phosphorylation. We identify on protein expression arrays novel cyclin E–Cdk2 substrates, including SIRT2, a member of the Sirtuin family of NAD+-dependent deacetylases that targets α-tubulin. We define Ser-331 as the site phosphorylated by cyclin E–Cdk2, cyclin A–Cdk2, and p35–Cdk5 both in vitro and in cells. Importantly, phosphorylation at Ser-331 inhibits the catalytic activity of SIRT2. Gain- and loss-of-function studies demonstrate that SIRT2 interfered with cell adhesion and cell migration. In postmitotic hippocampal neurons, neurite outgrowth and growth cone collapse are inhibited by SIRT2. The effects provoked by SIRT2, but not those of a nonphosphorylatable mutant, are antagonized by Cdk-dependent phosphorylation. Collectively, our findings identify a posttranslational mechanism that controls SIRT2 function, and they provide evidence for a novel regulatory circuitry involving Cdks, SIRT2, and microtubules.</jats:p>

dc.format.extent915-929
dc.format.mediumPrint
dc.languageen
dc.language.isoeng
dc.publisherRockefeller University Press
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectCatalytic Domain
dc.subjectCell Differentiation
dc.subjectCell Line
dc.subjectCell Movement
dc.subjectCyclin A
dc.subjectCyclin E
dc.subjectCyclin-Dependent Kinase 2
dc.subjectCyclin-Dependent Kinase 5
dc.subjectCyclin-Dependent Kinases
dc.subjectGrowth Cones
dc.subjectHeLa Cells
dc.subjectHippocampus
dc.subjectHumans
dc.subjectMice
dc.subjectMicrotubules
dc.subjectNerve Tissue Proteins
dc.subjectOncogene Proteins
dc.subjectPhosphorylation
dc.subjectProtein Processing, Post-Translational
dc.subjectSerine
dc.subjectSirtuin 2
dc.subjectSirtuins
dc.titleThe regulation of SIRT2 function by cyclin-dependent kinases affects cell motility
dc.typejournal-article
dc.typeJournal Article
dc.typeResearch Support, Non-U.S. Gov't
plymouth.author-urlhttps://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000254081100009&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=11bb513d99f797142bcfeffcc58ea008
plymouth.issue5
plymouth.volume180
plymouth.publication-statusPublished
plymouth.journalThe Journal of Cell Biology
dc.identifier.doi10.1083/jcb.200707126
plymouth.organisational-group/Plymouth
plymouth.organisational-group/Plymouth/Faculty of Health
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA/UoA01 Clinical Medicine
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA/UoA01 Clinical Medicine/UoA01 Clinical Medicine
plymouth.organisational-group/Plymouth/Research Groups
plymouth.organisational-group/Plymouth/Research Groups/Institute of Translational and Stratified Medicine (ITSMED)
plymouth.organisational-group/Plymouth/Research Groups/Institute of Translational and Stratified Medicine (ITSMED)/CBR
dc.publisher.placeUnited States
dc.identifier.eissn1540-8140
dc.rights.embargoperiodNot known
rioxxterms.versionofrecord10.1083/jcb.200707126
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.typeJournal Article/Review


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