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Substrate specificity of protein tyrosine phosphatase: Differential behavior of SHP-1 and SHP-2 towards signal regulation protein SIRPα1

✍ Scribed by Ashwini K. Mishra; Aihua Zhang; Tianqi Niu; Jian Yang; Xiaoshan Liang; Zhizhuang Joe Zhao; G. Wayne Zhou

Publisher
John Wiley and Sons
Year
2002
Tongue
English
Weight
137 KB
Volume
84
Category
Article
ISSN
0730-2312

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✦ Synopsis

Abstract

The substrate specificity of catalytic domains and the activation of full length protein tyrosine phosphatases, SHP‐1 and SHP‐2 have been investigated using synthetic phosphotyrosyl peptides derived from SIPRα1. We found that the catalytic domains of SHP‐1 and SHP‐2 exhibit different substrate specificity towards a longer trideca‐peptide pY^469+3^ (^−7^RPEDTLTpYADLDM^+5^) and not to the shorter decapeptide pY^469^ (^−5^EDTLTpYADLD^+4^), the former being the substrate of SHP‐2 only. Furthermore, the activation of full‐length SHP‐1 and not the SHP‐2 by the deca/trideca‐peptides suggested SIRPα 1 to be possibly acting as both an upstream activator and a substrate for SHP‐1, and merely as the downstream substrate for SHP‐2 in signaling events. J. Cell. Biochem. 84: 840–846, 2002. © 2002 Wiley‐Liss, Inc.

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