The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras.
Open accessAbstract
Protein-tyrosine-phosphatase SHPTP2 (Syp/PTP-1D/PTP2C) is the homologue of the Drosophila corkscrew (csw) gene product, which transmits positive signals from receptor tyrosine kinases. Likewise, SHPTP2 has been implicated in positive signaling from platelet-derived growth factor receptor beta (PDGFR). Upon PDGF stimulation, SHPTP2 binds to the PDGFR and becomes tyrosine-phosphorylated. We have identified tyrosine-542 (pY542TNI) as the major in vivo site of SHPTP2 tyrosine phosphorylation. The pY542TNI sequence conforms to the consensus binding site for the SH2 domain of Grb2, which, by association with Sos1, couples some growth factor receptors to Ras. Following PDGF stimulation, Grb2 binds tyrosine-phosphorylated SHPTP2. Moreover, a mutant PDGFR lacking its SHPTP2 binding site displays markedly reduced Grb2 binding. These data indicate that phosphorylation of SHPTP2 couples Grb2 to PDGFR in vivo, providing a mechanism for Ras activation by PDGFR and for positive signaling via SHPTP2 and Csw.
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“SHP2 is required for full activation of SOS1/2, whereas SOS1 inhibitors are inactive against SOS2.”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [142]
In the citing paper
“which is recruited to many receptor tyrosine kinases upon activation and is generally a positive regulator of Ras/MAPK signaling (Perkins et al., 1996; Bennett et al., 1994; Tang et al., 1995; Maroun et al., 2000; Oishi et al., 2006).”
From The Phosphatase SHP2 Regulates the Spacing Effect for Long-Term Memory Induction (2009) · cites this paper as Bennett et al., 1994
Citations
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The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1
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Phosphatidylinositol 3′‐kinase is activated by association with IRS‐1 during insulin stimulation.
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Cited by
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Protein modules and signalling networks
Pawson, T. (1995) · Nature · doi:10.1038/373573a0 · Cited by 2,420
Hyperactive Ras in developmental disorders and cancer
Schubbert, S., Shannon, K., & Bollag, G. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2109 · Cited by 1,583
RAS-targeted therapies: is the undruggable drugged?
Moore, A. R., Rosenberg, S. C., McCormick, F., & Malek, S. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0068-6 · Cited by 1,103
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Proteogenomic Characterization Reveals Therapeutic Vulnerabilities in Lung Adenocarcinoma
Gillette, M. A., Satpathy, S., Cao, S., Dhanasekaran, S. M., Vasaikar, S. V., Krug, K., Petralia, F., Li, Y., Liang, W.-W., Reva, B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.013 · Cited by 820
Metadata
- Authors
- Bennett, A. M., Tang, T. L., Sugimoto, S., Walsh, C. T., & Neel, B. G.
- Affiliations
- Beth Israel Deaconess Medical Center (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1994-07-19
- Volume
- 91
- Issue
- 15
- Pages
- 7335-7339
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC44394
- OpenAlex
- W2006147172
- Cited by
- 397
- References
- 43
- Citations by year
- 2026: 8 · 2025: 4 · 2024: 4 · 2023: 9 · 2022: 11 · 2021: 13 · 2020: 7 · 2019: 6 · 2018: 10 · 2017: 5 · 2016: 10 · 2015: 4 · 2014: 5 · 2013: 10 · 2012: 7
- FWCI
- 12.78
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Cancer Society
- National Institutes of Health (GM20011, CA49152)
- National Cancer Institute (CA-49152)
- National Institute of General Medical Sciences (GM 20011)
- 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 › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
- Keywords
- PDGFRβ, Ras activation, Grb2, SOS1, receptor tyrosine kinase signaling, tyrosine phosphorylation, SH2 domain binding
- MeSH terms
- Animals, Base Sequence, Binding Sites, Cell Line, DNA, Humans, Mice, Inbred BALB C, Molecular Sequence Data, Phosphorylation, Genes, ras, Signal Transduction, 3T3 Cells, Protein Tyrosine Phosphatases, Receptors, Platelet-Derived Growth Factor, Intracellular Signaling Peptides and Proteins, Mice, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatase, Non-Receptor Type 11, SH2 Domain-Containing Protein Tyrosine Phosphatases
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