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Presence of cyclic micleotide–Ca2+ independent protein kinase in bovine brain coated vesicles

Nature volume 298, pages 574–576 (1982)Cite this article

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.

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Authors and Affiliations

  1. Laboratory of Proteins, University of Paris V, CNRS ER 102,

    A. Pauloin, I. Bernier & P. Jollès

  2. INSERM Unité U-116, 45 rue des Saints-Pères, F75270, Paris, Cedex 06, France

    A. Pauloin, I. Bernier & P. Jollès

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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

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