Title : The C-terminal acidic motif of Phafin2 inhibits PH domain binding to phosphatidylinositol 3-phosphate.

Pub. Date : 2020 Jun 1

PMID : 32126233






6 Functional Relationships(s)
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1 The C-terminal acidic motif of Phafin2 inhibits PH domain binding to phosphatidylinositol 3-phosphate. phosphatidylinositol 3-phosphate pleckstrin homology and FYVE domain containing 2 Homo sapiens
2 Phafin2 is a phosphatidylinositol 3-phosphate (PtdIns3P)-binding effector involved in endosomal and lysosomal membrane-associated signaling. phosphatidylinositol 3-phosphate pleckstrin homology and FYVE domain containing 2 Homo sapiens
3 Phafin2 is a phosphatidylinositol 3-phosphate (PtdIns3P)-binding effector involved in endosomal and lysosomal membrane-associated signaling. phosphatidylinositol 3-phosphate pleckstrin homology and FYVE domain containing 2 Homo sapiens
4 Both the Phafin2 PH and the FYVE domains bind PtdIns3P, although their redundant function in the protein is unclear. phosphatidylinositol 3-phosphate pleckstrin homology and FYVE domain containing 2 Homo sapiens
5 Using site-directed mutagenesis and truncation constructs, we discovered that the Phafin2 FYVE domain is constitutive for PtdIns3P binding, whereas PH domain binding to PtdIns3P is autoinhibited by a conserved C-terminal acidic motif. phosphatidylinositol 3-phosphate pleckstrin homology and FYVE domain containing 2 Homo sapiens
6 These findings suggest that binding of the Phafin2 PH domain to PtdIns3P in membrane compartments occurs through a highly regulated mechanism. phosphatidylinositol 3-phosphate pleckstrin homology and FYVE domain containing 2 Homo sapiens