Phosphorylation of the purified CaCB-receptor
- PMID: 2469877
Phosphorylation of the purified CaCB-receptor
Abstract
The purified receptor for calcium channel blockers (CaCB-receptor) from rabbit skeletal muscle contains three polypeptides within a molecular mass of 165, 55, and 32 kDa. cAMP-dependent protein kinase was shown to phosphorylate preferentially the 165-kDa protein. The major phosphorylation site was identified and compared with the recently published primary sequence of the CaCB-receptor. It is concluded that serine 687 is the phosphorylation site. Phosphorylation of serine 687 may regulate the open-state probability of the CaCB-receptor.
Similar articles
-
Site-specific phosphorylation of the purified receptor for calcium-channel blockers by cAMP- and cGMP-dependent protein kinases, protein kinase C, calmodulin-dependent protein kinase II and casein kinase II.Eur J Biochem. 1988 Dec 15;178(2):535-42. doi: 10.1111/j.1432-1033.1988.tb14480.x. Eur J Biochem. 1988. PMID: 2850184
-
Reconstitution of the purified receptor for calcium channel blockers.Biomed Biochim Acta. 1987;46(8-9):S357-62. Biomed Biochim Acta. 1987. PMID: 2829861
-
Primary structure of the receptor for calcium channel blockers from skeletal muscle.Nature. 1987 Jul 23-29;328(6128):313-8. doi: 10.1038/328313a0. Nature. 1987. PMID: 3037387
-
[Calcium channels: structure and function of receptors for calcium channel blockers in skeletal muscle].Arzneimittelforschung. 1989 Jan;39(1A):164-8. Arzneimittelforschung. 1989. PMID: 2541734 Review. German.
-
L-type calcium channels in cardiac and skeletal muscle. Purification and phosphorylation.Ann N Y Acad Sci. 1989;560:27-38. doi: 10.1111/j.1749-6632.1989.tb24076.x. Ann N Y Acad Sci. 1989. PMID: 2545140 Review. No abstract available.