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 SIPRalpha1. 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 SIRPalpha 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.
Copyright 2002 Wiley‐Liss, Inc.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Antigens, Differentiation*
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Catalytic Domain / physiology
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Enzyme Activation
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Humans
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Intracellular Signaling Peptides and Proteins
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Kinetics
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Membrane Glycoproteins / chemistry
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Membrane Glycoproteins / metabolism*
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Neural Cell Adhesion Molecule L1*
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Neural Cell Adhesion Molecules / chemistry
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Neural Cell Adhesion Molecules / metabolism*
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Oligopeptides / chemical synthesis
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Oligopeptides / chemistry
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Oligopeptides / metabolism*
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Protein Tyrosine Phosphatase, Non-Receptor Type 11
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Protein Tyrosine Phosphatase, Non-Receptor Type 6
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Protein Tyrosine Phosphatases / genetics
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Protein Tyrosine Phosphatases / isolation & purification
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Protein Tyrosine Phosphatases / metabolism*
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Receptors, Immunologic*
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Substrate Specificity
Substances
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Antigens, Differentiation
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Intracellular Signaling Peptides and Proteins
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Membrane Glycoproteins
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Neural Cell Adhesion Molecule L1
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Neural Cell Adhesion Molecules
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Oligopeptides
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Receptors, Immunologic
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PTPN11 protein, human
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PTPN6 protein, human
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Protein Tyrosine Phosphatase, Non-Receptor Type 11
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Protein Tyrosine Phosphatase, Non-Receptor Type 6
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Protein Tyrosine Phosphatases