ArticleProtein science : a publication of the Protein Society2002
The SPOT technique as a tool for studying protein tyrosine phosphatase substrate specificities.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 40 citations in OpenAlex.
- GPSD: a hybrid learning framework for the prediction of phosphatase-specific dephosphorylation sites.Briefings in bioinformatics · 2024Article
- Article
- Both Intrinsic Substrate Preference and Network Context Contribute to Substrate Selection of Classical Tyrosine Phosphatases.The Journal of biological chemistry · 2017Article
- Protein-tyrosine phosphatase 1B (PTP1B) is a novel regulator of central brain-derived neurotrophic factor and tropomyosin receptor kinase B (TrkB) signaling.The Journal of biological chemistry · 2014Article
- Bacterial urease and its role in long-lasting human diseases.Current protein & peptide science · 2012Review
- Central regulation of metabolism by protein tyrosine phosphatases.Frontiers in neuroscience · 2012Article
- Deciphering enzyme function using peptide arrays.Molecular biotechnology · 2011Review
- Identification of new substrates of the protein-tyrosine phosphatase PTP1B by Bayesian integration of proteome evidence.The Journal of biological chemistry · 2011Article
- Phospho3D: a database of three-dimensional structures of protein phosphorylation sites.Nucleic acids research · 2007Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
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.
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