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PMID: 1454521 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Mutation of the casein kinase II phosphorylation site abolishes the anti-proliferative activity of p53.

Nucleic acids research ·Vol. 20 ·No. 21 ·1992-11-11 ·Pages 5565-70

Milne DM, Palmer RH, Meek DW

Abstract

The p53 tumour suppressor protein is phosphorylated by several protein kinases, including casein kinase II. In order to understand the functional significance of phosphorylation by casein kinase II, we have introduced mutations at serine 386 in mouse p53, the residue phosphorylated by this kinase, and investigated their effects on the ability of p53 to arrest cell growth. Replacement of serine 386 by alanine led to loss of growth suppressor activity, while aspartic acid at this position partially retained suppressor function. These data suggest that the anti-proliferative activity of p53 is activated by phosphorylation at serine 386, and establish a direct link between the covalent modification of a growth suppressor protein and regulation of its activity in mammalian cells.

MeSH Terms
3T3 Cells Animals Casein Kinase II Cell Division/genetics Cells, Cultured Cloning, Molecular Cricetinae Humans Mice Mutagenesis, Site-Directed Phosphorylation Protein Serine-Threonine Kinases/genetics,metabolism Rats Serine/metabolism Temperature Transfection Tumor Suppressor Protein p53/genetics,metabolism
Chemicals
Tumor Suppressor Protein p53 Serine Casein Kinase II Protein Serine-Threonine Kinases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Milne D M
Department of Biochemistry, University of Dundee, UK.
Palmer R H
Meek D W
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
Published
1992-11-11
Pages
5565-70
Language
English
Region
England
NLM ID
0411011
PMCID
PMC334387
Subset
IM
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