Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling
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SHPTP2 is a ubiquitously expressed tyrosine-specific protein phosphatase that contains two amino-terminal Src homology 2 (SH2) domains responsible for its association with tyrosine-phosphorylated proteins. In this study, expression of dominant interfering mutants of SHPTP2 was found to inhibit insulin stimulation of c-fos reporter gene expression and activation of the 42-kDa (Erk2) and 44-kDa (Erk1) mitogen-activated protein kinases. Cotransfection of dominant interfering SHPTP2 mutants with v-Ras or Grb2 indicated that SHPTP2 regulated insulin signaling either upstream of or in parallel to Ras function. Furthermore, phosphotyrosine blotting and immunoprecipitation identified the 125-kDa focal adhesion kinase (pp125FAK) as a substrate for insulin-dependent tyrosine dephosphorylation. These data demonstrate that SHPTP2 functions as a positive regulator of insulin action and that insulin signaling results in the dephosphorylation of tyrosine-phosphorylated pp125FAK.
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SHP2 catalytic activity is required for RAS/ERK pathway activation by most, if not all, RTKs, but its C-terminal tyrosyl residues are essential for only some RTK signaling pathways.
“SHP2 catalytic activity is required for RAS/ERK pathway activation by most, if not all, RTKs, but its C-terminal tyrosyl residues are essential for only some RTK signaling pathways (Araki et al., 2003; O’Reilly and Neel, 1998; Yamauchi et al., 1995).”
From SHP2 inhibition diminishes KRASG12C cycling and promotes tumor microenvironment remodeling (2021) · cites this paper as Yamauchi et al., 1995
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References 51 · Cited by 263
- Authors
- Yamauchi, K., Milarski, K. L., Saltiel, A. R., & Pessin, J. E.
- Affiliations
- University of Iowa (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1995-01-31
- Volume
- 92
- Issue
- 3
- Pages
- 664-668
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC42680
- OpenAlex
- W2029911977
- Cited by
- 263
- References
- 51
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2022: 2 · 2021: 3 · 2020: 2 · 2019: 1 · 2018: 1 · 2017: 4 · 2016: 2 · 2015: 5 · 2014: 4 · 2013: 2 · 2012: 5
- FWCI
- 13.50
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- protein tyrosine phosphatase, insulin signaling, c-fos transcription, Ras, Grb2, focal adhesion kinase, tyrosine dephosphorylation, SH2 domain
- MeSH terms
- Animals, Cell Extracts, Cricetinae, Insulin, Mutation, Phosphorylation, Protein-Tyrosine Kinases, Proteins, Transcription, Genetic, Transfection, Tyrosine, Signal Transduction, Cell Adhesion Molecules, CHO Cells, Genes, fos, Protein Tyrosine Phosphatases, Calcium-Calmodulin-Dependent Protein Kinases, Genes, Reporter, DNA, Complementary, ras Proteins, Phosphotyrosine, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinases, Intracellular Signaling Peptides and Proteins, Mitogen-Activated Protein Kinase 3, Adaptor Proteins, Signal Transducing, GRB2 Adaptor Protein, Focal Adhesion Protein-Tyrosine Kinases, Focal Adhesion Kinase 1, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatase, Non-Receptor Type 11
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