Calalb M B, Kincaid R L, Soderling T R
Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37232.
Biochem Biophys Res Commun. 1990 Oct 30;172(2):551-6. doi: 10.1016/0006-291x(90)90708-u.
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.
利用一种包含钙调蛋白（CaM）结合结构域和丝氨酸磷酸化位点的合成肽，研究了钙调磷酸酶磷酸化对其与钙调蛋白（CaM）结合的影响。该肽对应于脑钙调磷酸酶A亚基的391 - 414位氨基酸残基，可被蛋白激酶C和Ca2+/CaM依赖性蛋白激酶II快速磷酸化，但不能被cAMP依赖性蛋白激酶磷酸化。与未磷酸化的肽相比，391 - 414肽的磷酸化并未显著改变其与CaM的结合。
