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dc.contributor.authorKong, Yahui
dc.contributor.authorCui, Hang
dc.contributor.authorZhang, Hong
dc.date2022-08-11T08:11:05.000
dc.date.accessioned2022-08-23T17:33:07Z
dc.date.available2022-08-23T17:33:07Z
dc.date.issued2011-12-01
dc.date.submitted2012-04-26
dc.identifier.citationAging Cell. 2011 Dec;10(6):1038-46. doi: 10.1111/j.1474-9726.2011.00746.x. Epub 2011 Oct 7.
dc.identifier.issn1474-9726
dc.identifier.doi10.1111/j.1474-9726.2011.00746.x
dc.identifier.pmid21933340
dc.identifier.urihttp://hdl.handle.net/20.500.14038/51099
dc.description.abstractThe inhibitor of differentiation or DNA binding (Id) family of transcription regulators plays an important role in cell proliferation, differentiation, and senescence. However, regulation of Id expression during these processes is poorly understood. Id proteins are known to undergo rapid turnover mediated by the ubiquitin-proteasome pathway. Anaphase-promoting complex has been shown to ubiquitinate Id2, but E3 ubiquitin ligase(s) that ubiquitinate other Id family members are not known. Here, we report for the first time the identification of Smurf2 as the E3 ligase that ubiquitinates Id1 and Id3. Smurf2-mediated ubiquitination and consequent degradation of Id1 or Id3 plays an important role in the regulation of Id expression in senescent cells. Furthermore, we found that Id1 is the mediator through which Smurf2 regulates p16 expression, providing a mechanistic link between Smurf2 and p16 expression during senescence.
dc.language.isoen_US
dc.publisherBlackwell Pub.
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=21933340&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1111/j.1474-9726.2011.00746.x
dc.subjectCell Aging
dc.subjectCell Differentiation
dc.subjectCell Line, Tumor
dc.subjectCell Proliferation
dc.subjectFibroblasts
dc.subjectGene Expression Regulation
dc.subjectGenetic Vectors
dc.subjectHumans
dc.subjectInhibitor of Differentiation Protein 1
dc.subjectInhibitor of Differentiation Proteins
dc.subjectLentivirus
dc.subjectNeoplasm Proteins
dc.subjectReal-Time Polymerase Chain Reaction
dc.subjectSignal Transduction
dc.subjectTransfection
dc.subjectUbiquitin
dc.subjectUbiquitin-Protein Ligase Complexes
dc.subjectUbiquitin-Protein Ligases
dc.subjectUbiquitination
dc.subjectCell Biology
dc.titleSmurf2-mediated ubiquitination and degradation of Id1 regulates p16 expression during senescence
dc.typeJournal Article
dc.source.journaltitleAging cell
dc.source.volume10
dc.source.issue6
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/zhang/11
dc.identifier.contextkey2799843
html.description.abstract<p>The inhibitor of differentiation or DNA binding (Id) family of transcription regulators plays an important role in cell proliferation, differentiation, and senescence. However, regulation of Id expression during these processes is poorly understood. Id proteins are known to undergo rapid turnover mediated by the ubiquitin-proteasome pathway. Anaphase-promoting complex has been shown to ubiquitinate Id2, but E3 ubiquitin ligase(s) that ubiquitinate other Id family members are not known. Here, we report for the first time the identification of Smurf2 as the E3 ligase that ubiquitinates Id1 and Id3. Smurf2-mediated ubiquitination and consequent degradation of Id1 or Id3 plays an important role in the regulation of Id expression in senescent cells. Furthermore, we found that Id1 is the mediator through which Smurf2 regulates p16 expression, providing a mechanistic link between Smurf2 and p16 expression during senescence.</p>
dc.identifier.submissionpathzhang/11
dc.contributor.departmentDepartment of Cell Biology
dc.source.pages1038-46


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