SHIP2 associates with intersectin and recruits it to the plasma membrane in response to EGF |
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Authors: | Xie Jingwei Vandenbroere Isabelle Pirson Isabelle |
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Affiliation: | Institute of Interdisciplinary Research (IRIBHM), School of Medicine, Free University of Brussels, Campus Erasme, Building C, Route de Lennik 808, B-1070 Brussels, Belgium. |
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Abstract: | 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. STRUCTURED SUMMARY: |
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Keywords: | SHIP2, SH2 domain containing inositol polyphosphate 5-phosphatase 2 ITSN, intersectin HA, hemagglutinin GST, glutathione S-transferase ERK, extracellular signal-regulated kinase EGF, epidermal growth factor EGFR, epidermal growth factor receptor JNK, c-Jun NH2-terminal kinase EH, Eps15 homology SH3, Src homology 3 MAPK, mitogen activated protein kinase Sos, sonof-sevenless |
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