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Endocytosis is driven by a mechanism which is characterized by an orderly
congregation of a large number of proteins which effectuate, first, formation of
a coated vesicles, second, pinching off the vesicle and, third, regulated
transport. True to the nature of many other proteins involved in multimolecular
complexes, also endocytosis-associated proteins, such as Eps15, clathrin and
AP-2, are characterized by distinct domains which mediate the protein-protein
interactions. We now report that a group of well-established endocytosis and/or
vesicular trafficking proteins possess a VHS domain, a recently described domain
with an unknown function. We suggest that in these proteins VHS serves as a
membrane targeting domain which by its specific features together with FYVE, SH3
and/or TAM domains, which are also present in some VHS-containing proteins, is
involved in the stage-specific assembly of the endocytic machinery.
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