Reversibility of coated vesicle dissociation.
The dissociation of the coated vesicles to clathrin and uncoated vesicles and their reassociation have been studied under various conditions. The extent of reassociation is pH dependent and increases slightly with increasing concentrations of the components. Unlike the self-association of clathrin which is strongly salt dependent, the reassociation of clathrin and uncoated vesicles is practically independent of salt concentration. The coated vesicle gradually loses its coat with increasing pH, and the dissociation process is not an all or none reaction. Ca2+ inhibits dissociation of the coated vesicles and enhances the reassociation of clathrin and uncoated vesicles. Our results show that, although many conditions result in reassociation of protein and lipid vesicle, few conditions result in vesicles of both the same size and composition as native coated vesicles.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002417:Cattle; D002499:Centrifugation, Density Gradient; D002966:Clathrin; D003034:Coated Pits, Cell-Membrane / Q000378:metabolism*; D011992:Endosomes / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008027:Light; D008565:Membrane Proteins / Q000378:metabolism; D012542:Scattering, Radiation; D013050:Spectrometry, Fluorescence
D002966:Clathrin; D008565:Membrane Proteins; D002118:Calcium