PMID: 8612628Mar 1, 1996Paper

A comparative study of the phosphotyrosyl phosphatase specificity of protein phosphatase type 2A and phosphotyrosyl phosphatase type 1B using phosphopeptides and the phosphoproteins p50/HS1, c-Fgr and Lyn

European Journal of Biochemistry
P AgostinisJ Goris

Abstract

The phosphotyrosyl phosphatase (PTPase) specificity of phosphotyrosyl-phosphatase-activator-(PTPA)-stimulated protein phosphatase (PP)2A(D) (rabbit muscle) and a bona fide PTP-1B (Xenopus laevis oocytes) were examined in vitro using phosphotyrosine-containing peptides, derived from the phosphorylation sites of p34cdc2, p50/HS1 protein, Abl, c-Src and c-Fgr, as well as the intact phosphoprotein p50/HS1 and the Src-related tyrosine kinases, Lyn and c-Fgr. The local specificity determinants were found to be different for both PTPases. The length of the phosphopeptides is more important for PP2A(D) than for PTP-1B, C-terminal acidic residues adjacent to the phosphotyrosine are detrimental for the PTPase activity of PP2A(D), but they do not affect the PTP-1B activity. Acidic residues at the --2 and --3 position relative to Tyr(P) primarily dictate dephosphorylation by PTP-1B. The higher-order structure of the protein substrates also differentially influences both enzymes: the phospho-octapeptide KDDEYpNPA, which reproduces the autophosphorylation site in c-Fgr (Tyr400), is only dephosphorylated by PP2A(D) if embedded in the intact protein, whereas the opposite is true for PTP-1B. Both the intact p50/HS1 phosphoprotein and the derive...Continue Reading

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Citations

Nov 5, 1998·Bioorganic & Medicinal Chemistry·S D TaylorZ Huang
Aug 19, 2006·Molecular Cell·Yang ChaoYigong Shi
Jul 5, 2007·American Journal of Physiology. Regulatory, Integrative and Comparative Physiology·Katherine A SheehanR John Solaro
Mar 17, 1998·Biochemical and Biophysical Research Communications·A M BrunatiA Donella-Deana
Apr 21, 1999·Biochimica Et Biophysica Acta·Q WangC Ramachandran
Nov 14, 1997·Biochimica Et Biophysica Acta·G Ramponi, M Stefani

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