HDM2 negatively affects the Chk2-mediated phosphorylation of p53.
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.
Mesh Terms:
Animals, Blotting, Western, COS Cells, Catalysis, Cercopithecus aethiops, Gene Expression, Glutathione Transferase, Humans, Nuclear Proteins, Phosphorylation, Precipitin Tests, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-mdm2, Recombinant Proteins, Transfection, Tumor Suppressor Protein p53
Animals, Blotting, Western, COS Cells, Catalysis, Cercopithecus aethiops, Gene Expression, Glutathione Transferase, Humans, Nuclear Proteins, Phosphorylation, Precipitin Tests, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-mdm2, Recombinant Proteins, Transfection, Tumor Suppressor Protein p53
FEBS Lett.
Date: May. 09, 2005
PubMed ID: 15862297
View in: Pubmed Google Scholar
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