Premium
VHS domain marks a group of proteins involved in endocytosis and vesicular trafficking
Author(s) -
Lohi Olli,
Lehto Veli-Pekka
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01401-x
Subject(s) - endocytosis , endocytic cycle , microbiology and biotechnology , clathrin , vesicle , vesicular transport protein , transport protein , biology , function (biology) , chemistry , biochemistry , membrane , receptor
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.