Abstract:
:The glycogen-binding (G) subunit of protein phosphatase-1G is phosphorylated stoichiometrically by glycogen synthase kinase-3 (GSK3), and with a greater catalytic efficiency than glycogen synthase, but only after prior phosphorylation by cyclic AMP-dependent protein kinase (A-kinase) at site 1. The residues phosphorylated are the first two serines in the sequence AIFKPGFSPQPSRRGS-, while the C-terminal serine (site 1) is one of the two residues phosphorylated by A-kinase. These findings demonstrate that (i) the G subunit undergoes multisite phosphorylation in vitro; (ii) phosphorylation by GSK3 requires the presence of a C-terminal phosphoserine residue; (iii) GSK3 can synergise with protein kinases other than casein kinase-2.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Dent P,Campbell DG,Hubbard MJ,Cohen Pdoi
10.1016/0014-5793(89)80433-8subject
Has Abstractpub_date
1989-05-08 00:00:00pages
67-72issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(89)80433-8journal_volume
248pub_type
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