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- 6673604: ITSN-1S (uniprotkb: Q15811-2) and SHIP2 (uniprotkb: O15357) colocalize (MI: 0403) by fluorescence microscopy (MI: 0416) MINT- 6673646, MINT- 6694843: SHIP2 (uniprotkb: Q6P549) physically interacts (MI: 0218) with ITSN-1S (uniprotkb: Q9Z0R4-2) by anti bait coimmunoprecipitation (MI: 0006) MINT- 6673386: SHIP2 (uniprotkb: O15357) physically interacts (MI: 0218) with ITSN-1S (uniprotkb: Q15811-2) by two hybrid (MI: 0018) MINT- 6673429, MINT- 6673447, MINT- 6673475: ITSN-1S (uniprotkb: Q15811-2) physically interacts (MI: 0218) with SHIP2 (uniprotkb: O15357) by anti tag coimmunoprecipitation (MI: 0007) MINT- 6673513, MINT- 6673542, MINT- 6673557, MINT- 6673572: ITSN-1S (uniprotkb: Q15811-2) physically interacts (MI: 0218) with SHIP2 (uniprotkb: O15357) by pull down (MI: 0096) MINT- 6673462: ITSN-1L (uniprotkb: Q15811-1) physically interacts (MI: 0218) with SHIP2 (uniprotkb: O15357) by anti tag coimmunoprecipitation (MI: 0007)

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