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Title

SIAH-mediated ubiquitination and degradation of acetyl-transferases regulate the p53 response and protein acetylation

AuthorsGrishina, Inna; Dubus, Katherina; García-Limones, Carmen; Shneider, Constanze; Shresta, Amit; García, Carlos; Calzado, Marco A.; Schmitz, M. Lienhard
KeywordsUbiquitin E3 ligase
P53
Protein acetylation
HIPK2
SIAH
Issue Date2012
PublisherElsevier
CitationBiochimica et Biophysica Acta - Molecular Cell Research 1823: 2287- 2296 (2012)
AbstractPosttranslational modification of proteins by lysine acetylation regulates many biological processes ranging from signal transduction to chromatin compaction. Here we identify the acetyl-transferases CBP/p300, Tip60 and PCAF as new substrates for the ubiquitin E3 ligases SIAH1 and SIAH2. While CBP/p300 can undergo ubiquitin/proteasome-dependent degradation by SIAH1 and SIAH2, the two other acetyl-transferases are exclusively degraded by SIAH2. Accordingly, SIAH-deficient cells show enhanced protein acetylation, thus revealing SIAH proteins as indirect regulators of the cellular acetylation status. Functional experiments show that Tip60/PCAF-mediated acetylation of the tumor suppressor p53 is antagonized by the p53 target gene SIAH2 which mediates ubiquitin/proteasome-mediated degradation of both acetyl-transferases and consequently diminishes p53 acetylation and transcriptional activity. The p53 kinase HIPK2 mediates hierarchical phosphorylation of SIAH2 at 5 sites, which further boosts its activity as a ubiquitin E3 ligase for several substrates and therefore dampens the late p53 response. © 2012 Elsevier B.V.
URIhttp://hdl.handle.net/10261/114636
DOI10.1016/j.bbamcr.2012.09.011
Identifiersdoi: 10.1016/j.bbamcr.2012.09.011
issn: 0167-4889
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