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HDM2 negatively affects the Chk2‐mediated phosphorylation of p53
Author(s) -
Bjørling-Poulsen Marina,
Meek David,
Issinger Olaf-Georg
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.081
Subject(s) - phosphorylation , immunoprecipitation , transfection , recombinant dna , p53 protein , microbiology and biotechnology , chemistry , biochemistry , biology , gene
By GST pull downs and co‐immunoprecipitation analyses we found that recombinant Chk2 and HDM2 can form stable complexes in vitro. Chk2/HDM2 complexes were also detected in transfected Cos‐1 cells over‐expressing both proteins. Furthermore, we show that HDM2, as would be expected, severely affects the Chk2‐catalyzed phosphorylation of p53. HDM2 itself is only slightly phosphorylated by Chk2. However, whereas HDM2 inhibits the Chk2‐catalyzed p53 phosphorylation, HDM2 phosphorylation by Chk2 doubles in the presence of p53. The significance of the HDM2 phosphorylation is unknown, but it is possible that it might influence the stability of the HDM2/p53 complex.