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Brain Coated Vesicle Destabilization and Phosphorylation of Coat Proteins
Author(s) -
GeorgievaHanson Veneta,
Schook William J.,
Puszkin Saul
Publication year - 1988
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1988.tb13265.x
Subject(s) - melittin , vesicle , vesicle fusion , egta , phosphorylation , biophysics , biochemistry , chemistry , biology , microbiology and biotechnology , synaptic vesicle , calcium , membrane , organic chemistry
Two basic polypeptides, bee venom melittin and poly‐L‐lysine, induced concentration‐dependent destabilization of bovine brain coated vesicles. Ultrastructurally the changes observed were aggregation of clathrin coats and segregation of the vesicle membrane, concomitant with the appearance of elongated cisternae of various sizes. Changes in coated vesicle morphology induced by melittin and poly‐L‐lysine were concurrent with stimulation of phosphate incorporation in proteins of the coat lattice: M, 33,000 and 100,000. Melittin‐stimulated phosphorylation was Ca 2+ sensitive and inhibited by EGTA. The initiation of vesicle membrane segregation by melittin, followed by fusion and formation of elongated membrane cisternae, paralleled an increase of endogenous phospholipase A 2 activity. The data suggest that a correlation exists between the state of assembly of the coat proteins on coated vesicles and protein phosphorylation.