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| Content Provider | PubMed Central |
|---|---|
| Author | Lu, Chengrong Zhu, Feng Cho, Yong-yeon Tang, Faqing Zykova, Tatyana Ma, Wei-ya Bode, Ann M. Dong, Zigang |
| Abstract | Immunofluorescence studies have revealed that H2AX is phosphorylated at the sites of DNA double-strand breaks induced by ionizing radiation and is required for recruitment of repair factors into nuclear foci after DNA damage. Therefore the function of H2AX is believed to be associated primarily with repair of DNA damage. Here we report a function of H2AX in cellular apoptosis. Our data showed that H2AX is phosphorylated by UVA-activated JNK. We also provided evidence showing that UVA induces caspase-3 and caspase-activated DNAse (CAD) activity in both H2AX wildtype and H2AX knockout mouse embryonic fibroblasts (MEFs). However, DNA fragmentation occurred only in H2AX wildtype MEFs. Furthermore, H2AX phosphorylation was critical for DNA degradation triggered by CAD in vitro. Taken together, these data indicated that H2AX phosphorylation is required for DNA ladder formation, but not for the activation of caspase-3; and the JNK/H2AX pathway cooperates with the caspase-3/CAD pathway resulting in cellular apoptosis. |
| Related Links | http://dx.doi.org/10.1016/j.molcel.2006.05.023 |
| Ending Page | 132 |
| Page Count | 12 |
| Starting Page | 121 |
| File Format | |
| ISSN | 10972765 |
| Journal | Molecular cell |
| Issue Number | 1 |
| Volume Number | 23 |
| Language | English |
| Publisher Date | 2006-07-01 |
| Access Restriction | Open |
| Subject Keyword | Cell Biology Molecular Biology Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Molecular Biology |
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