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Biochem Biophys Res Commun. 2006 Sep 22;348(2):367-73. Epub 2006 Jul 28.

A novel redox-based switch: LMW-PTP oxidation enhances Grb2 binding and leads to ERK activation.

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  • 1Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Florence, Italy.


Low molecular weight-PTP has been reported as a redox-sensitive protein during both platelet-derived growth factor and integrin signalling. In response to oxidation the phosphatase undergoes a reversible inactivation, which in turn leads to the increase in tyrosine phosphorylation of its substrates and the properly executed anchorage-dependent proliferation program. Here, we report that an exogenous oxidative stress enhances LMW-PTP tyrosine phosphorylation, through oxidation/inactivation of the enzyme, thus preventing its auto-dephosphorylation activity. In particular, we observed a selective hyper-phosphorylation of Tyr132, that acts as a docking site for the adaptor protein Grb2. The redox-dependent enhancement of Grb2 recruitment to LMW-PTP ultimately leads to an improvement of ERK activation, likely triggering a prosurvival signal against the oxidant environment.

[PubMed - indexed for MEDLINE]
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