title: 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.
authors: Physiologische Chemie, Medizinische Fakultät, Universität des Saarlandes, F.R.G.
authors: A
authors: A
authors: Röhrkasten
authors: W
authors: W
authors: Nastainczyk
authors: M
authors: M
authors: Sieber
authors: H
authors: H
authors: Jahn
authors: S
authors: S
authors: Regulla
authors: F
authors: F
authors: Hofmann
mesh_terms: D000818:Animals; D015220:Calcium Channels; D006801:Humans; D010766:Phosphorylation; D011978:Receptors, Nicotinic / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D015220:Calcium Channels; D011978:Receptors, Nicotinic