VHS domain marks a group of proteins involved in endocytosis and vesicular trafficking.
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.
Lohi
O
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Department of Pathology, University of Oulu, Finland.
Lehto
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VP
D000595:Amino Acid Sequence; D001665:Binding Sites; D001692:Biological Transport; D004705:Endocytosis; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000502:physiology*; D017386:Sequence Homology, Amino Acid
D011506:Proteins