Premium
Regulation of yeast phosphorylase by phosphorylase kinase and cAMP‐dependent protein kinase
Author(s) -
Wingender-Drissen Ruth,
Becker Jörn Ullrich
Publication year - 1983
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(83)81156-9
Subject(s) - phosphorylase kinase , glycogen phosphorylase , mitogen activated protein kinase kinase , cyclin dependent kinase 9 , map2k7 , map kinase kinase kinase , phosphorylation , biochemistry , cyclin dependent kinase 2 , chemistry , ask1 , protein kinase a , kinase , microbiology and biotechnology , biology , enzyme
Yeast phosphorylase is phosphorylated and activated by a cyclic AMP‐independent protein kinase (called phosphorylase kinase) and a cyclic AMP‐dependent protein kinase. Only in the presence of both kinases is phosphorylase fully activated and phosphorylated. No evidence was found for the presence of two phosphorylation sites as an identical phosphopeptide pattern of phosphorylase is obtained after phosphorylation by either one or both kinases. The kinases probably phosphorylate identical sites but recognize different subunits of phosphorylase. Phosphorylase kinase phosphorylates the high‐ M r subunit while cAMP‐dependent protein kinase phosphorylates the low‐ M r subunit.