Serum starvation induces H2AX phosphorylation to regulate apoptosis via p38 MAPK pathway.

Abstract:

:Phosphorylation of H2AX is believed to be associated with the repair of damaged DNA. Recent findings suggest a novel function of H2AX in cellular apoptosis. Specifically, it was shown that ultraviolet A-activated JNK phosphorylates H2AX to regulate apoptosis. Here we show that serum starvation induces H2AX phosphorylation and apoptosis independent of the JNK pathway. Serum starvation induced p38 phosphorylation, whereas it did not affect the phosphorylation of ERK or JNK. Inhibition of p38 reduced H2AX phosphorylation and apoptosis. Furthermore, p38 was found to phosphorylate H2AX directly in vitro and was colocalized with H2AX in vivo. Finally, we demonstrate that H2AX phosphorylation is required for serum starvation-induced apoptosis. Taken together, these data elucidate a novel signaling pathway (p38/H2AX) to regulate apoptosis.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Lu C,Shi Y,Wang Z,Song Z,Zhu M,Cai Q,Chen T

doi

10.1016/j.febslet.2008.06.051

subject

Has Abstract

pub_date

2008-08-06 00:00:00

pages

2703-8

issue

18

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(08)00574-7

journal_volume

582

pub_type

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