Calmodulin binding and protein phosphorylation in adrenal medulla coated vesicles

FEBS Letters

Burgoyne, Robert D.¹  Geisow, Michael J.¹ 

[1] National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, England

关键词: Ca2+ calmodulin;    Chromaffin cell;    Phosphorylation;    Adrenal medulla;    Clathrin;    Coated vesicle;   

DOI  :  10.1016/0014-5793(84)80303-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Coated vesicles from bovine adrenal medulla contained clathrin and major detergent-insoluble polypeptides of 120-100, 51 and 49 kDa. Intact coated vesicles and vesicles lacking clathrin light chains were bound by immobilized calmodulin in the presence of Ca²⁺. Clathrin in the form of 700 Å cages was not bound. The calmodulin binding components in intact coated vesicles are therefore contributed by the enclosed vesicle or by the 120-100, 50 or 49 kda polypeptides. The 51 kDa component incorporated ³²P_i from labelled ATP by an endogenous kinase activity; no other coat or vesicle membrane protein was phosphorylated in vitro, either by intrinsic or exogenous kinases.

【 授权许可】

Unknown