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SHIP1/2 interaction with tyrosine phosphorylated peptides mimicking an immunoreceptor signalling motif.

par Pesesse, Xavier ;Backers, Katrien ;Moreau, Colette ;Zhang, Jing ;Blero, Daniel ;Paternotte, Nathalie ;Erneux, Christophe
Référence Advances in enzyme regulation, 46, page (142-153)
Publication Publié, 2006

Article révisé par les pairs

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Résumé :

SHIP1/2 are SH2 domains containing inositol 5-phosphatases and are expressed in both non-hematopoietic and hematopoietic cells. SHIP1/2 are recruited via their SH2 domain by several Fc immunoreceptors comprising ITAMs, ITIMs and also directly to some tyrosine kinase receptors. Using a series of tyrosine phosphorylated peptides, we show that SHIP2 interacts, in vitro, with the ITAM-like peptide GGDGpYYDLSPL. These interactions could be shown with recombinant tSHIP2 (containing the SH2 and catalytic domain of SHIP2) or with the SH2 domain of SHIP2 alone produced in bacteria. The immobilized tyrosine phosphorylated peptides could also be used to isolate the endogenous SHIP1 and SHIP2 present in B- and T cells. Moreover, they have been used to identify SHIP2 in A-20 B cells and HeLa cells. In CHO-IR, SHIP2 was tyrosine phosphorylated in response to insulin. In this model, the phosphorylated SHIP2 could be adsorbed to the tyrosine phosphorylated peptide but the amount of affinity trapped enzyme was unaffected when SHIP2 was tyrosine phosphorylated. These results indicate that the two members of the SHIP family could interact in vitro to tyrosine phosphorylated peptides with the ITAM consensus of pYXXL. The interaction also provides a method for the rapid isolation of SHIP1 and SHIP2 5-phosphatases in an active state. © 2006 Elsevier Ltd. All rights reserved.