Document Detail


Protein tyrosine phosphatase SHP-2: a proto-oncogene product that promotes Ras activation.
MedLine Citation:
PMID:  19622105     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
SHP-2 is a cytoplasmic protein tyrosine phosphatase (PTP) that contains two Src homology 2 (SH2) domains. Although PTPs are generally considered to be negative regulators on the basis of their ability to oppose the effects of protein tyrosine kinases, SHP-2 is unusual in that it promotes the activation of the Ras-MAPK signaling pathway by receptors for various growth factors and cytokines. The molecular basis for the activation of SHP-2 is also unique: In the basal state, the NH(2)-terminal SH2 domain of SHP-2 interacts with the PTP domain, resulting in autoinhibition of PTP activity; the binding of SHP-2 via its SH2 domains to tyrosine-phosphorylated growth factor receptors or docking proteins, however, results in disruption of this intramolecular interaction, leading to exposure of the PTP domain and catalytic activation. Indeed, SHP-2 proteins with artificial mutations in the NH(2)-terminal SH2 domain have been shown to act as dominant active mutants in vitro. Such activating mutations of PTPN11 (human SHP-2 gene) were subsequently identified in individuals with Noonan syndrome, a human developmental disorder that is sometimes associated with juvenile myelomonocytic leukemia. Furthermore, somatic mutations of PTPN11 were found to be associated with pediatric leukemia. SHP-2 is also thought to participate in the development of other malignant disorders, but in a manner independent of such activating mutations. Biochemical and functional studies of SHP-2 and genetic analysis of PTPN11 in human disorders have thus converged to provide new insight into the pathogenesis of cancer as well as potential new targets for cancer treatment.
Authors:
Takashi Matozaki; Yoji Murata; Yasuyuki Saito; Hideki Okazawa; Hiroshi Ohnishi
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Publication Detail:
Type:  Journal Article; Review     Date:  2009-06-23
Journal Detail:
Title:  Cancer science     Volume:  100     ISSN:  1349-7006     ISO Abbreviation:  Cancer Sci.     Publication Date:  2009 Oct 
Date Detail:
Created Date:  2009-09-21     Completed Date:  2009-10-09     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101168776     Medline TA:  Cancer Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  1786-93     Citation Subset:  IM    
Affiliation:
Laboratory of Biosignal Sciences, Institute for Molecular and Cellular Regulation, Gunma University, Maebashi, Gunma, Japan. matozaki@showa.gunma-u.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Animals
Enzyme Activation / physiology
Humans
Neoplasms / genetics,  metabolism*
Protein Tyrosine Phosphatase, Non-Receptor Type 11 / genetics,  metabolism*
Signal Transduction / physiology*
ras Proteins / metabolism*
Chemical
Reg. No./Substance:
EC 3.1.3.48/Protein Tyrosine Phosphatase, Non-Receptor Type 11; EC 3.6.5.2/ras Proteins

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