Regulation of protein tyrosine phosphatase 1C: opposing effects of the two src homology 2 domains
摘要：
The regulatory roles of the two homology 2 () domains of were investigated by comparing recombinant full-length with mutants in which either the N-terminal (N-) domain (delta NSH2), the C-terminal (C-) domain (delta ) or both domains were deleted (delta NSH2 delta ). This revealed that the domains have opposing and independent effects on activity: strong inhibition by N-(42-fold) and weak activation by C-(2.1-fold). C-caused activation across a wide pH range while N-inhibited most at neutral and high pH through a shift of the basic limb of the pH profile of kcat/Km, apparently via perturbation of an active-site pKa value. A phosphotyrosyl derived from the erythropoietin receptor caused an approximately 30-fold activation of and delta but had no effect on delta NSH2 or delta NSH2 delta , indicating that of this to N-abolished its inhibition. Since C-separates N-from the catalytic domain in full-length and activation is observed for delta , it appears that the inhibitory effect of N-is independent of the position in the sequence and that intermolecular interactions may also be possible.
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DOI：
10.1093/protein/8.12.1309
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