Title : Lysosomal interaction of Akt with Phafin2: a critical step in the induction of autophagy.

Pub. Date : 2014

PMID : 24416124






6 Functional Relationships(s)
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1 A sucrose gradient fractionation experiment revealed that both Akt and Phafin2 co-existed in the same lysosome enriched fraction after autophagy induction. Sucrose pleckstrin homology and FYVE domain containing 2 Homo sapiens
2 BiFC analysis using PtdIns (3)P interaction defective mutant of Phafin2 demonstrated that lysosomal accumulation of the Akt-Phafin2 complex and subsequent induction of autophagy were lysosomal PtdIns (3)P dependent events. phosphatidylinositol 3-phosphate pleckstrin homology and FYVE domain containing 2 Homo sapiens
3 BiFC analysis using PtdIns (3)P interaction defective mutant of Phafin2 demonstrated that lysosomal accumulation of the Akt-Phafin2 complex and subsequent induction of autophagy were lysosomal PtdIns (3)P dependent events. phosphatidylinositol 3-phosphate pleckstrin homology and FYVE domain containing 2 Homo sapiens
4 BiFC analysis using PtdIns (3)P interaction defective mutant of Phafin2 demonstrated that lysosomal accumulation of the Akt-Phafin2 complex and subsequent induction of autophagy were lysosomal PtdIns (3)P dependent events. phosphatidylinositol 3-phosphate pleckstrin homology and FYVE domain containing 2 Homo sapiens
5 BiFC analysis using PtdIns (3)P interaction defective mutant of Phafin2 demonstrated that lysosomal accumulation of the Akt-Phafin2 complex and subsequent induction of autophagy were lysosomal PtdIns (3)P dependent events. phosphatidylinositol 3-phosphate pleckstrin homology and FYVE domain containing 2 Homo sapiens
6 Taken together, these findings establish that lysosomal accumulation of Akt and Phafin2 is a critical step in the induction of autophagy via an interaction with PtdIns (3)P. phosphatidylinositol 3-phosphate pleckstrin homology and FYVE domain containing 2 Homo sapiens