TY - JOUR
T1 - ERKs and p38 kinases mediate ultraviolet B-induced phosphorylation of histone H3 at serine 10
AU - Zhong, Shu Ping
AU - Ma, Wei-Ya
AU - Dong, Zigang
PY - 2000/7/14
Y1 - 2000/7/14
N2 - Histone H3 is the core protein of the nucleosome. Phosphorylation of H3 involves immediate early gene expression, chromatic remodeling, and chromosome condensation during mitosis. Very recently, Rsk2 or MSK1 kinase- mediated phospholation of H3 at serene 10 was reported. In the present study, we show that both ERKs and p38 kinase may mediate ultraviolet B-induced phosphorylation of H3 at serine 10. PD 98059, a MEK1 inhibitor, and SB 202190, a p38 kinase inhibitor, efficiently inhibited ultraviolet B-induced phosphorylation of H3. Phosphorylation of H3 was also inhibited in cells expressing dominant negative mutant (DNM) ERK2 and DNM p38 kinase. In contrast, no inhibition of H3 phosphorylation in Jnk1 or Jnk2 knockout cells (Jnkl(-/-) or Jnk2(-/-)) and cells expressing DNM JNK1 was observed. More importantly, incubation of active ERK2 or p38 kinase with H3 protein resulted in phosphorylation of H3 at serine 10 in vitro. These results suggest that ERK and p38 kinase are at least two important mediators of phosphorylation of H3 at serine 10.
AB - Histone H3 is the core protein of the nucleosome. Phosphorylation of H3 involves immediate early gene expression, chromatic remodeling, and chromosome condensation during mitosis. Very recently, Rsk2 or MSK1 kinase- mediated phospholation of H3 at serene 10 was reported. In the present study, we show that both ERKs and p38 kinase may mediate ultraviolet B-induced phosphorylation of H3 at serine 10. PD 98059, a MEK1 inhibitor, and SB 202190, a p38 kinase inhibitor, efficiently inhibited ultraviolet B-induced phosphorylation of H3. Phosphorylation of H3 was also inhibited in cells expressing dominant negative mutant (DNM) ERK2 and DNM p38 kinase. In contrast, no inhibition of H3 phosphorylation in Jnk1 or Jnk2 knockout cells (Jnkl(-/-) or Jnk2(-/-)) and cells expressing DNM JNK1 was observed. More importantly, incubation of active ERK2 or p38 kinase with H3 protein resulted in phosphorylation of H3 at serine 10 in vitro. These results suggest that ERK and p38 kinase are at least two important mediators of phosphorylation of H3 at serine 10.
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U2 - 10.1074/jbc.M909934199
DO - 10.1074/jbc.M909934199
M3 - Article
C2 - 10806218
AN - SCOPUS:0034647733
SN - 0021-9258
VL - 275
SP - 20980
EP - 20984
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 28
ER -