Brain coated vesicle destabilization and phosphorylation of coat proteins.
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: Mr 33,000 and 100,000. Melittin-stimulated phosphorylation was Ca2+ 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 A2 activity. The data suggest that a correlation exists between the state of assembly of the coat proteins on coated vesicles and protein phosphorylation.
D000818:Animals; D001921:Brain / Q000648:ultrastructure*; D002118:Calcium / Q000494:pharmacology; D002417:Cattle; D002966:Clathrin / Q000378:metabolism*; D003034:Coated Pits, Cell-Membrane / Q000187:drug effects / Q000648:ultrastructure*; D011992:Endosomes / Q000648:ultrastructure*; D004790:Enzyme Induction / Q000187:drug effects; D008555:Melitten / Q000494:pharmacology; D008854:Microscopy, Electron; D008970:Molecular Weight; D010710:Phosphates / Q000378:metabolism*; D010741:Phospholipases A / Q000096:biosynthesis; D054467:Phospholipases A2; D010766:Phosphorylation; D011107:Polylysine / Q000494:pharmacology
D002966:Clathrin; D010710:Phosphates; D008555:Melitten; D011107:Polylysine; D010741:Phospholipases A; D054467:Phospholipases A2; D002118:Calcium