MAP Kinases Mediate UVB-induced Phosphorylation of Histone H3 at Serine 28

Shuping Zhong, Yiguo Zhang, Cheryl Jansen, Hidemasa Goto, Masaki Inagaki, Zigang Dong

Research output: Contribution to journalArticlepeer-review

51 Scopus citations

Abstract

Histone H3 phosphorylation is related closely to chromatin remodeling and chromosome condensation. H3 phosphorylation at serine 28 is coupled with mitotic chromosome condensation in diverse mammalian cell lines. However, the pathway that mediates phosphorylation of H3 at serine 28 is unknown. In the present study, ERK1, ERK2, or p38 kinase strongly phosphorylated H3 at serine 28 in vitro. JNK1 or JNK2 was able also to phosphorylate H3 at serine 28 in vitro but to a lesser degree. UVB irradiation markedly induced phosphorylation of H3 at serine 28 in JB6 Cl 41 cells. PD 98059, a MEK1 inhibitor, and SB 202190, a p38 kinase inhibitor, efficiently repressed UVB-induced H3 phosphorylation at serine 28. Expression of dominant negative mutant (DNM) ERK2 in JB6 Cl 41 cells totally blocked UVB-induced phosphorylation of H3 at serine 28. Additionally, DNM p38 kinase or DNM JNK1 partially blocked UVB-induced H3 phosphorylation at serine 28. Furthermore, UVB-induced H3 phosphorylation at serine 28 was inhibited in Jnk1-/- cells but not in Jnk2 -/- cells. These results suggest that UVB-induced H3 phosphorylation at serine 28 may be mediated by mitogen-activated protein kinases.

Original languageEnglish (US)
Pages (from-to)12932-12937
Number of pages6
JournalJournal of Biological Chemistry
Volume276
Issue number16
DOIs
StatePublished - Apr 20 2001

Fingerprint

Dive into the research topics of 'MAP Kinases Mediate UVB-induced Phosphorylation of Histone H3 at Serine 28'. Together they form a unique fingerprint.

Cite this