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A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1.
Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, OR 97201, USA.
Phosphorylation of the human p53 protein at Ser-392 has been shown to be responsive to UV but not gamma irradiation. Here we describe identification and purification of a mammalian UV-activated protein kinase complex that phosphorylates Ser-392 of p53 in vitro. This kinase complex contains casein kinase 2 (CK2) and the chromatin transcriptional elongation factor FACT (a heterodimer of hSpt16 and SSRP1). In vitro studies show that FACT alters the specificity of CK2 in the complex such that it selectively phosphorylates p53 over other substrates including casein. In addition, phosphorylation by the kinase complex enhances p53 activity. These results thus provide a potential mechanism for p53 activation by UV irradiation.
PMID: 11239457 [PubMed - indexed for MEDLINE]
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Cited by 21 PubMed Central articles
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FACT facilitates chromatin transcription by RNA polymerases I and III.
Birch JL, Tan BC, Panov KI, Panova TB, Andersen JS, Owen-Hughes TA, Russell J, Lee SC, Zomerdijk JC.
EMBO J. 2009 Apr 8; 28(7):854-65. Epub 2009 Feb 12.
[EMBO J. 2009]
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AIMP2/p38, the scaffold for the multi-tRNA synthetase complex, responds to genotoxic stresses via p53.
Han JM, Park BJ, Park SG, Oh YS, Choi SJ, Lee SW, Hwang SK, Chang SH, Cho MH, Kim S.
Proc Natl Acad Sci U S A. 2008 Aug 12; 105(32):11206-11. Epub 2008 Aug 11.
[Proc Natl Acad Sci U S A. 2008]
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Unraveling protein networks with power graph analysis.
Royer L, Reimann M, Andreopoulos B, Schroeder M.
PLoS Comput Biol. 2008 Jul 11; 4(7):e1000108. Epub 2008 Jul 11.
[PLoS Comput Biol. 2008]
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