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Protein kinase CK1 is a p53‐threonine 18 kinase which requires prior phosphorylation of serine 15
Author(s) -
Dumaz Nicolas,
Milne Diane M,
Meek David W
Publication year - 1999
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/s0014-5793(99)01647-6
Subject(s) - casein kinase 1 , phosphorylation , threonine , serine , casein kinase 2 , biochemistry , protein phosphorylation , kinase , map2k7 , casein kinase 2, alpha 1 , protein kinase a , chemistry , biology , microbiology and biotechnology , cyclin dependent kinase 2
p53 is a potent transcription factor which is regulated by sequential multisite phosphorylation and acetylation. In this paper, we identify threonine 18 of p53, a key site in regulating the interaction between p53 and its regulatory partner MDM2, as a novel site phosphorylated in vitro by purified recombinant casein kinase 1 (CK1) δ. Strikingly, phosphorylation of threonine 18 is dependent upon prior phosphorylation of serine 15. These data highlight an additional and physiologically important target residue for CK1 in p53 and suggest a potential mechanism by which sequential modification of a pivotal N‐terminal residue in p53 may occur following stress‐activated modification of serine 15.