VHS domain marks a group of proteins involved in endocytosis and vesicular trafficking

FEBS Lett. 1998 Dec 4;440(3):255-7. doi: 10.1016/s0014-5793(98)01401-x.


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.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Biological Transport
  • Endocytosis*
  • Humans
  • Molecular Sequence Data
  • Protein Conformation
  • Proteins / chemistry
  • Proteins / physiology*
  • Sequence Homology, Amino Acid


  • Proteins