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

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Giannoni E,Raugei G,Chiarugi P,Ramponi G

doi

10.1016/j.bbrc.2006.07.091

subject

Has Abstract

pub_date

2006-09-22 00:00:00

pages

367-73

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)01543-9

journal_volume

348

pub_type

杂志文章

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