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Calmodulin‐dependent multiprotein kinase and protein kinase C phosphorylate the same site on HMG‐CoA reductase as the AMP‐activated protein kinase
Author(s) -
Clarke Paul R.,
Grahame Hardie D.
Publication year - 1990
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 - 10.1016/0014-5793(90)81157-j
Subject(s) - map2k7 , mitogen activated protein kinase kinase , protein kinase a , map kinase kinase kinase , cyclin dependent kinase 9 , cyclin dependent kinase 2 , biochemistry , chemistry , c raf , phosphorylation , microbiology and biotechnology , biology
Calmodulin‐dependent multiprotein kinase and protein kinase C phosphorylate and inactivate both intact, microsomal HMG‐CoA reductase, and the purified 53 kDa catalytic fragment. Isolation of the single phosphopeptide produced by combined cleavage with cyanogen bromide and Lys‐C proteinase reveals that this is due to phosphorylation of a single serine residue near the C‐terminus, corresponding to serine‐872 in the human enzyme. This is identical with the single serine phosphorylated by the AMP‐activated protein kinase. The nature of the protein kinase responsible for phosphorylation of this site in vivo is discussed.