Endocytosis is driven by a mechanism which is characterized by an orderly c
ongregation of a large number of proteins which effectuate, first, formatio
n of a coated vesicles, second, pinching off the vesicle and, third, regula
ted transport, True to the nature of many other proteins involved in multim
olecular complexes, also endocytosis-associated proteins, such as Eps15, cl
athrin and AP-2, are characterized by distinct domains which mediate the pr
otein-protein interactions, We now report that a group of well-established
endocytosis and/or vesicular trafficking proteins possess a VHS domain, a r
ecently described domain with an unknown function. We suggest that in these
proteins VHS serves as a membrane targeting domain which by its specific f
eatures 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. (C) 1998 Federation of European Biochemical So
cieties.