Cited by 397Protein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase SignalingCytokine Signaling Pathways and Interactions

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Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras.

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Bennett, A M, Tang, T L, Sugimoto, S, Walsh, C T, Neel, B G·1994·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.91.15.7335PMC PMC44394

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Abstract

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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Authors: Bennett, A. M., Tang, T. L., Sugimoto, S., Walsh, C. T., & Neel, B. G.
Affiliations: Beth Israel Deaconess Medical Center (US)
ORCID: Bennett, A M
Walsh, C T
Neel, B G
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
DOI: 10.1073/pnas.91.15.7335
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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Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras.

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