Abstract:
:Glycogen synthase kinase-5 (casein kinase-II) phosphorylates glycogen synthase on a serine termed site 5. This residue is just C-terminal to the 3 serines phosphorylated by glycogen synthase kinase-3, which are critical for the hormonal regulation of glycogen synthase in vivo. Although phosphorylation of site 5 does not affect the catalytic activity, it is demonstrated that this modification is a prerequisite for phosphorylation by glycogen synthase kinase-3. Since site 5 is almost fully phosphorylated in vivo under all conditions, the role of glycogen synthase kinase-5 would appear to be a novel one in forming the recognition site for another protein kinase.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Picton C,Woodgett J,Hemmings B,Cohen Pdoi
10.1016/0014-5793(82)81332-xsubject
Has Abstractpub_date
1982-12-13 00:00:00pages
191-6issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(82)81332-Xjournal_volume
150pub_type
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