Smurf2-mediated ubiquitination and degradation of Id1 regulates p16 expression during senescence
UMass Chan Affiliations
Department of Cell BiologyDocument Type
Journal ArticlePublication Date
2011-12-01Keywords
Cell AgingCell Differentiation
Cell Line, Tumor
Cell Proliferation
Fibroblasts
Gene Expression Regulation
Genetic Vectors
Humans
Inhibitor of Differentiation Protein 1
Inhibitor of Differentiation Proteins
Lentivirus
Neoplasm Proteins
Real-Time Polymerase Chain Reaction
Signal Transduction
Transfection
Ubiquitin
Ubiquitin-Protein Ligase Complexes
Ubiquitin-Protein Ligases
Ubiquitination
Cell Biology
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Show full item recordAbstract
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.Source
Aging Cell. 2011 Dec;10(6):1038-46. doi: 10.1111/j.1474-9726.2011.00746.x. Epub 2011 Oct 7.DOI
10.1111/j.1474-9726.2011.00746.xPermanent Link to this Item
http://hdl.handle.net/20.500.14038/51099PubMed ID
21933340Related Resources
Link to article in PubMedae974a485f413a2113503eed53cd6c53
10.1111/j.1474-9726.2011.00746.x
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