Presence of cyclic micleotide–ca2+ independent protein kinase in bovine brain coated vesicles

ABSTRACT Coated vesicles, which are membrane vesicles enclosed by a polyhedral protein lattice, are involved in many cellular events1–6, including intracellular membrane transport and

protein secretion, in which they must be able to undergo repeated membrane fusion and fission. The icosahedral lattice of protein surrounding the core of coated vesicles is composed

predominantly of clathrin, a 180,000 (180 K) molecular weight protein, and other 30 K and 36 K polypeptides7,8. In native conditions, the basic subunit of the coat consists of a trimer of

clathrin with probably three polypeptides of 30K and/or 36K (refs 9–11). Additional minor proteins of 100K and 55K have been reported in purified coated vesicles12. We describe here the

presence of cyclic nucleotide- and Ca2+-independent protein kinase activity in coated vesicles. This protein kinase phosphorylates specifically a unique 50K protein which can be co-purified

with clathrin and seems to be an integral protein of coated vesicles. Access through your institution Buy or subscribe This is a preview of subscription content, access via your institution

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SYNAPTOPHYSIN AND SYNAPSIN IN THE GENERATION OF SYNAPTIC VESICLE-LIKE CLUSTERS IN NON-NEURONAL CELLS Article Open access 11 January 2021 REFERENCES * Friend, D. S. & Farquhar, M. G. _J.

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Laboratory of Proteins, University of Paris V, CNRS ER 102, A. Pauloin, I. Bernier & P. Jollès * INSERM Unité U-116, 45 rue des Saints-Pères, F75270, Paris, Cedex 06, France A. Pauloin,

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permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Pauloin, A., Bernier, I. & Jollès, P. Presence of cyclic micleotide–Ca2+ independent protein kinase in bovine brain coated vesicles.

_Nature_ 298, 574–576 (1982). https://doi.org/10.1038/298574a0 Download citation * Received: 05 October 1981 * Accepted: 09 June 1982 * Issue Date: 05 August 1982 * DOI:

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