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

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 induc...

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Bibliographic Details
Published in:FEBS letters 2008-08, Vol.582 (18), p.2703-2708
Main Authors: Lu, Chengrong, Shi, Ying, Wang, Zhe, Song, Zhihong, Zhu, Meicai, Cai, Qing, Chen, Tao
Format: Article
Language:English
Subjects:
Animals
Apoptosis
Cell Line
H2AX
Histones - genetics
Histones - metabolism
Humans
ionizing radiation
MAPK
MAPKs
MEFs
Mice
mitogen-activated protein kinases
mouse embryonic fibroblasts
p38
p38 Mitogen-Activated Protein Kinases - metabolism
Phosphorylation
Serum
TBST
Tris-buffered saline containing Tween 20
ultraviolet
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2008.06.051