The Protein Tyrosine Phosphatase SHP-2 Regulates Interleukin-1-induced ERK Activation in Fibroblasts *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 278, Issue: 29, Page: 27190-27198
2003
- 36Citations
- 19Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations36
- Citation Indexes36
- 36
- CrossRef33
- Captures19
- Readers19
- 19
Article Description
Focal adhesion complexes are actin-rich, cytoskeletal structures that mediate cell adhesion to the substratum and also selectively regulate signal transduction pathways required for interleukin (IL)-1β signaling to the MAP kinase, ERK. IL-1-induced ERK activation is markedly diminished in fibroblasts deprived of focal adhesions whereas activation of p38 and JNK is unaffected. While IL-1 signaling is known to involve the activity of protein and lipid kinases including MAP kinases, FAK, and PI3K, little is known about the role of phosphatases in the regulation of IL-1 signal generation and attenuation. Here we demonstrate that SHP-2, a protein tyrosine phosphatase present in focal adhesions, modulates IL-1-induced ERK activation and the transient actin stress fiber disorganization that occurs following IL-1 treatment in human gingival fibroblasts. Using a combination of immunoblotting, immunoprecipitation, and immunostaining we show that SHP-2 is present in nascent focal adhesions and undergoes phosphorylation on tyrosine 542 in response to IL-1 stimulation. Blocking anti-SHP-2 antibodies, electoporated into the cytosol of fibroblasts, inhibited IL-1-induced ERK activation, actin filament assembly, and cell contraction, indicating a role for SHP-2 in these processes. In summary, our data indicate that SHP-2, a focal adhesion-associated protein, participates in IL-1-induced ERK activation likely via an adaptor function.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820846869; http://dx.doi.org/10.1074/jbc.m213083200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0038373277&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/12721296; http://www.jbc.org/lookup/doi/10.1074/jbc.M213083200; https://syndication.highwire.org/content/doi/10.1074/jbc.M213083200; https://linkinghub.elsevier.com/retrieve/pii/S0021925820846869; https://dx.doi.org/10.1074/jbc.m213083200
American Society for Biochemistry & Molecular Biology (ASBMB)
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