MAPKs and Mst1/Caspase-3 pathways contribute to H2B phosphorylation during UVB-induced apoptosis |
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Authors: | ChengRong Lu Ying Shi Yuan Luo LianNing Duan Yong Hou HongBo Hu Zhe Wang PeiDe Xiang |
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Institution: | (1) Department of Biotechnology, Indian Institute of Technology, Kharagpur, 721302, India;(2) School of Medical Science and Technology, Indian Institute of Technology, Kharagpur, India; |
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Abstract: | Apoptosis is a highly coordinated or programmed cell suicide mechanism in eukaryotes. Histone modification is associated with
nuclear events in apoptotic cells. Specifically H2B phosphorylation at serine 14 (Ser14) catalyzed by Mst1 kinase has been
linked to chromatin condensation during apoptosis. We report that activation of MAPKs (ERK1/2, JNK1/2 and p38) together with
Mst1 and caspase-3 is required for phosphorylation of H2B (Ser14) during ultraviolet B light (UVB)-induced apoptosis. UVB
can trigger activation of MAPKs and induce H2B phosphorylation at Ser14 but not acetylation in a time-dependent manner. Inhibition
of ERK1/2, JNK1/2 or p38 activity blocked H2B phosphorylation (Ser14). Furthermore, caspase-3 was activated by UVB to regulate
Mst1 activity, which phosphorylates H2B at Ser14, leading to chromatin condensation. Full inhibition of caspase-3 activity
reduced Mst1 activation and partially inhibited H2B phosphorylation (Ser14), but ERK1/2, JNK1/2 and p38 activities were not
affected. Taken together, these data revealed that H2B phosphorylation is regulated by both MAPKs and caspase-3/Mst1 pathways
during UVB-induced apoptosis. |
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Keywords: | apoptosis H2B MAPK Mst1 |
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