SHIP2 associates with intersectin and recruits it to the plasma membrane in response to EGF.
We identified intersectin1 (ITSN1) as a new binding partner of the SH2 domain containing inositol 5-phosphatase 2 (SHIP2). The interaction between SHIP2 and ITSN1 was confirmed in vivo. Src homology 3D, A, C, and E domains of ITSN1 were shown to be implicated in the interaction. In response to epidermal growth factor, SHIP2 expression could recruit the ITSN1 short form (ITSN1-S) to the cell membrane, while SHIP2 overexpression did not modulate the ITSN-mediated extracellular signal-regulated kinase1/2 and c-Jun NH2-terminal kinase activation. Our data provide a molecular link between SHIP2 and ITSN1 which are involved in receptor endocytosis regulation.
Xie
Jingwei
J
Institute of Interdisciplinary Research, Free University of Brussels, Route de Lennik 808, B-1070 Brussels, Belgium.
Vandenbroere
Isabelle
I
Pirson
Isabelle
I
D033942:Adaptor Proteins, Vesicular Transport / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D019556:COS Cells; D002462:Cell Membrane / Q000378:metabolism*; D002522:Chlorocebus aethiops; D004705:Endocytosis / Q000187:drug effects; D004815:Epidermal Growth Factor / Q000494:pharmacology; D006801:Humans; D000072183:Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
D033942:Adaptor Proteins, Vesicular Transport; C115919:intersectin 1; D004815:Epidermal Growth Factor; D010744:Phosphoric Monoester Hydrolases; C098706:INPPL1 protein, human; D000072183:Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases