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The SPOT technique as a tool for studying protein tyrosine phosphatase substrate specificities.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Huguenin-Reggiani, Martine Hooft van Huijsduijnen, Rob Espanel, Xavier
Description	Country affiliation: Switzerland Author Affiliation: Espanel X ( Serono Pharmaceutical Research Institute, 14, chemin des Aulx, 1228 Plan-Les-Ouates, Geneva, Switzerland.)
Abstract	The activity of protein tyrosine phosphatases (PTPs) is restricted by their substrate specificities. The analysis of PTP specificity was greatly helped by the discovery that 'substrate-trapping' PTP mutants, such as PTP-1B D181A, stably and specifically bind their substrates. We have set up a PTP substrate specificity assay based on the SPOT technique, which involves the microsynthesis of (phospho)peptides on membranes. To validate this approach, substrate trapping PTP-1B was tested on its cognate ligand, the autophosphorylated insulin receptor (IR). On SPOT membranes, IR peptides with phosphotyrosine 1163 were efficiently bound by PTP1B D181A, and dephosphorylated by PTP-1B. Phosphotyrosine 1163 was preferred over the neighboring 1158 and 1162 phosphotyrosines. PTP-1B also recognized IR-like motifs in Trk autophosphorylation domains, and STAT 5 phosphopeptides. Using a gridded 20-by-20 SPOT library, we show that peptides with the YZM motif (Z: phosphotyrosine) are the strongest ligands for PTP-1B D181A, but not the optimal substrates for dephosphorylation by wild-type PTP1B. In addition we show that PTP-1B and PTP-beta dephosphorylation efficiency is strongly modulated by the introduction of phospho-serine or phospho-threonine in their cognate phospho-tyrosine substrates. Altogether our data illustrate that the SPOT technique is a highly efficient tool for the study of PTP substrate specificity.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	10
Volume Number	11
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2002-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Protein Tyrosine Phosphatases Metabolism Amino Acid Motifs Peptide Library Phosphopeptides Chemical Synthesis Phosphorylation Receptor, Insulin Substrate Specificity Physiology Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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