Journal
CELLULAR SIGNALLING
Volume 14, Issue 3, Pages 219-229Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/S0898-6568(01)00241-8
Keywords
SHP1; SlIP2; IL-3; Gab-2; PIR-B; IL-3 receptor; substrate-trapping
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SHP1 and SHP2 tyrosine phosphatases have both been implicated in signalling pathways downstream of the interleukin-3 (IL-3) reccptor. We have investigated the cc-association of SHP1 and SHP2 with tyrosine-phosphorylated proteins in IL-3-dependent BaF/3 cells. We demonstrate that both SHP1 and SHP2 associate with Aic2A (beta chain of the IL-3 receptor), Gab2 and the paired inhibitory receptor B (PIR-B). The individual SH2 domains of SHP2 can independently bind Gab2, potentially important for the adapter function of SHP2. Association of both phosphatases with Aic2A and Gab2 increases upon IL-3 treatment. Recruitment of SHP1 to PIR-B also increases in response to IL-3, suggesting a functional link between inhibitory and cytokine receptor signalling. Aic2A is a rapid target for dephosphorylation following IL-3 stimulation and substrate-trapping versions of both phosphatases identify Aic2A and Gab2 as substrates for SHP1 and SHP2. These studies suggest that SH2-domain interactions are important for targetting these phosphatases to their substrates. (C) 2002 Elsevier Science Inc. All rights reserved.
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