TY - JOUR
T1 - Substrate specificity of liver calmodulin-dependent glycogen synthase kinase
AU - Schworer, Charles M.
AU - Soderling, Thomas R.
N1 - Funding Information:
work was supported
PY - 1983/10/31
Y1 - 1983/10/31
N2 - A number of proteins were tested as potential substrates for purified rabbit liver calmodulin-dependent glycogen synthase kinase. It was found that liver phenylalanine hydroxylase and several brain proteins including tyrosine hydroxylase, microtubule-associated protein 2, and synapsin I were readily phosphorylated. Brain tubulin was very poorly phosphorylated. These results suggest that calmodulin-dependent glycogen synthase kinase may be a more general protein kinase involved in the regulation of several cellular Ca2+-dependent functions.
AB - A number of proteins were tested as potential substrates for purified rabbit liver calmodulin-dependent glycogen synthase kinase. It was found that liver phenylalanine hydroxylase and several brain proteins including tyrosine hydroxylase, microtubule-associated protein 2, and synapsin I were readily phosphorylated. Brain tubulin was very poorly phosphorylated. These results suggest that calmodulin-dependent glycogen synthase kinase may be a more general protein kinase involved in the regulation of several cellular Ca2+-dependent functions.
UR - http://www.scopus.com/inward/record.url?scp=0021116680&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0021116680&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(83)90538-7
DO - 10.1016/0006-291X(83)90538-7
M3 - Article
C2 - 6140005
AN - SCOPUS:0021116680
SN - 0006-291X
VL - 116
SP - 412
EP - 416
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -