SHIP2 associates with intersectin and recruits it to the plasma membrane in response to EGF

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

MINT-6673513, MINT-6673542, MINT-6673557,MINT-6673572:

Abbreviations: 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

Keywords: SHIP2, Intersectin, EGF, Endocytosis, MAPK, Scaffold protein