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Oxidation of cofilin mediates T cell hyporesponsiveness under oxidative stress conditions.

Abstract：

:Oxidative stress leads to impaired T cell activation. A central integrator of T cell activation is the actin-remodelling protein cofilin. Cofilin is activated through dephosphorylation at Ser3. Activated cofilin enables actin dynamics through severing and depolymerization of F-actin. Binding of cofilin to actin is required for formation of the immune synapse and T cell activation. Here, we showed that oxidatively stressed human T cells were impaired in chemotaxis- and costimulation-induced F-actin modulation. Although cofilin was dephosphorylated, steady-state F-actin levels increased under oxidative stress conditions. Mass spectrometry revealed that cofilin itself was a target for oxidation. Cofilin oxidation induced formation of an intramolecular disulfide bridge and loss of its Ser3 phosphorylation. Importantly, dephosphorylated oxidized cofilin, although still able to bind to F-actin, did not mediate F-actin depolymerization. Impairing actin dynamics through oxidation of cofilin provides a molecular explanation for the T cell hyporesponsiveness caused by oxidative stress.

journal_name

Immunity

journal_title

Immunity

authors

Klemke M,Wabnitz GH,Funke F,Funk B,Kirchgessner H,Samstag Y

doi

10.1016/j.immuni.2008.06.016

subject

Has Abstract

pub_date

2008-09-19 00:00:00

pages

404-13

issue

3

eissn

1074-7613

issn

1097-4180

pii

S1074-7613(08)00369-5

journal_volume

29

pub_type

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