Calmodulin binding and protein phosphorylation in adrenal medulla coated vesicles |
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Authors: | M J Geisow R D Burgoyne |
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Institution: | National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, England |
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Abstract: | 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 A 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 32Pi 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. |
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Keywords: | Chromaffin cell Phosphorylation Adrenal medulla Clathrin Coated vesicle |
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