摘要：

The FYVE finger domain was demonstrated to bind to phosphatidylinositol-3-phosphate (PtdIns(3)P). Data obtained provided in vivo evidence that the FYVE finger was a conserved domain that interacted with 3'-phosphoinositide. It was also found that the FYVE fingers of the early-endosomal autoantigen EEA1 and the endosomal protein Hrs bound directly and specifically to PtdIns(3)P, an activity that required bound Zn2+. Further evidence indicated that the structure and function of FYVE fingers are evolutionarily conserved and that FYVE fingers are vital structural elements in a subset of proteins that regulate endocytic/vacuolar membrane traffic.

展开