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  • Title: PH domain-mediated membrane targeting of Asef.
    Author: Muroya K, Kawasaki Y, Hayashi T, Ohwada S, Akiyama T.
    Journal: Biochem Biophys Res Commun; 2007 Mar 30; 355(1):85-8. PubMed ID: 17292853.
    Abstract:
    The APC-associated guanine nucleotide exchange factor (GEF) Asef regulates cell morphology and migration. Asef contains a pleckstrin homology (PH) domain in addition to Dbl homology (DH), APC-binding (ABR), and Src homology 3 (SH3) domains. Here we show that the PH domain of Asef binds to phosphatidylinositol 3,4,5-trisphophate [PtdIns(3,4,5)P3] and targets Asef to the cell-cell adhesion sites in MDCK II cells. Furthermore, we demonstrate that overexpression of Asef in MDCK II cells results in increases in the amounts of E-cadherin and the actin filaments at the sites of cell-cell contact. These results suggest that Asef is targeted via its PH domain to the cell-cell adhesion sites and is involved in the regulation of cell adhesion.
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