Shp-2 Tyrosine Phosphatase: Signaling One Cell or Many
Abstract
Shp-2, a widely expressed cytoplasmic tyrosine phosphatase with two src-homology 2 (SH2) domains, has received much attention in the signal transduction field recently. Significant progress has been made in understanding the structure and function of this phosphatase, together with its Drosophila homologue, Corkscrew, as well as the close relative Shp-1 tyrosine phosphatase. The crystal structure of Shp-2 revealed an autoinhibitory mechanism of the catalytic activity by the N-terminal SH2 domain. Shp-2 apparently participates in signaling events downstream of receptors for growth factors, cytokines, hormones, antigens, and extracellular matrixes in the control of cell growth, differentiation, migration, and death. Shp-2 is an important molecule that integrates signals among various cytoplasmic pathways and may also couple intracellular and intercellular information flow.
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Possible tyrosine phosphatases include an unidentified nuclear tyrosine phosphatase activity that inactivates IFN-gamma-stimulated STAT-1 and the SH2-containing phosphatases SHP-1 and SHP-2, which regulate cytokine signals in other tissues.
“Possible tyrosine phosphatases include an unidentified nuclear tyrosine phosphatase activity that has been reported to inactivate IFN-γ-stimulated STAT-1 (37) and the SH2-containing phosphatases, SHP-1 and SHP-2, which regulate cytokine signals in other tissues (38).”
From Expression of suppressors of cytokine signaling during liver regeneration (2001) · cites this paper as [38]
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Self-citation
- Authors
- Feng, G.-S.
- Affiliations
- Indiana University Indianapolis (US)
- Corresponding author
- Feng, Gen-Sheng
- ORCID
- Feng, Gen-Sheng
- Venue
- Experimental Cell Research
- Publisher
- Elsevier BV
- Published
- 1999-11
- Volume
- 253
- Issue
- 1
- Pages
- 47-54
- ISSN
- 0014-4827 (ISSN-L)
- OpenAlex
- W1987403356
- Cited by
- 285
- References
- 3
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 3 · 2023: 3 · 2022: 6 · 2021: 6 · 2020: 2 · 2019: 6 · 2018: 2 · 2017: 6 · 2016: 4 · 2015: 4 · 2014: 11 · 2013: 7 · 2012: 13
- FWCI
- 5.18
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Experimental Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (R01CA078606, R01CA78606)
- National Institute of General Medical Sciences (R29GM53660, R29GM053660)
- 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
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Keywords
- SHP2, protein tyrosine phosphatase, SH2 domain, autoinhibition, SHP-1, corkscrew, signal transduction, growth factor receptors, cytokine receptors, hormone receptors, extracellular matrix receptors, cell growth, cell differentiation, cell migration, cell death, signal integration
- MeSH terms
- Models, Biological, Signal Transduction, Protein Tyrosine Phosphatases, src Homology Domains, Intracellular Signaling Peptides and Proteins, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatase, Non-Receptor Type 11, SH2 Domain-Containing Protein Tyrosine Phosphatases
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