Abstract:
:SHP1 and SHP2 tyrosine phosphatases have both been implicated in signalling pathways downstream of the interleukin-3 (IL-3) receptor. We have investigated the co-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.
journal_name
Cell Signaljournal_title
Cellular signallingauthors
Wheadon H,Paling NR,Welham MJdoi
10.1016/s0898-6568(01)00241-8subject
Has Abstractpub_date
2002-03-01 00:00:00pages
219-29issue
3eissn
0898-6568issn
1873-3913pii
S0898656801002418journal_volume
14pub_type
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journal_title:Cellular signalling
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journal_title:Cellular signalling
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journal_title:Cellular signalling
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journal_title:Cellular signalling
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pub_type: 杂志文章
doi:10.1016/0898-6568(94)00041-7
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pub_type: 杂志文章
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journal_title:Cellular signalling
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journal_title:Cellular signalling
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pub_type: 杂志文章
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