TY - JOUR
T1 - Phosphorylation of calcineurin
T2 - Effect on calmodulin binding
AU - Calalb, Mihail B.
AU - Kincaid, Randall L.
AU - Soderling, Thomas R.
N1 - Funding Information:
by NIH grant
PY - 1990/10/30
Y1 - 1990/10/30
N2 - The effect of phosphorylation of calcineurin on calmodulin (CaM) binding was examined using a synthetic peptide which contains the CaM-binding domain and the serine phosphorylation site. The peptide, corresponding to residues 391-414 of brain calcineurin A subunit, was rapidly phosphorylated by protein kinase C and Ca2+ CaM-dependent protein kinase II but not by cAMP-dependent protein kinase. Phosphorylation of peptide 391-414 did not significantly alter the binding of CaM when compared to the non-phosphorylated peptide.
AB - The effect of phosphorylation of calcineurin on calmodulin (CaM) binding was examined using a synthetic peptide which contains the CaM-binding domain and the serine phosphorylation site. The peptide, corresponding to residues 391-414 of brain calcineurin A subunit, was rapidly phosphorylated by protein kinase C and Ca2+ CaM-dependent protein kinase II but not by cAMP-dependent protein kinase. Phosphorylation of peptide 391-414 did not significantly alter the binding of CaM when compared to the non-phosphorylated peptide.
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U2 - 10.1016/0006-291X(90)90708-U
DO - 10.1016/0006-291X(90)90708-U
M3 - Article
C2 - 2173570
AN - SCOPUS:0025075371
SN - 0006-291X
VL - 172
SP - 551
EP - 556
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -