دورية أكاديمية
BAZ1B is dispensable for H2AX phosphorylation on Tyrosine 142 during spermatogenesis
العنوان: | BAZ1B is dispensable for H2AX phosphorylation on Tyrosine 142 during spermatogenesis |
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المؤلفون: | Tyler J. Broering, Yuan-Liang Wang, Ram Naresh Pandey, Rashmi S. Hegde, Shao-Chun Wang, Satoshi H. Namekawa |
المصدر: | Biology Open, Vol 4, Iss 7, Pp 873-884 (2015) |
بيانات النشر: | The Company of Biologists, 2015. |
سنة النشر: | 2015 |
المجموعة: | LCC:Science LCC:Biology (General) |
مصطلحات موضوعية: | Meiosis, Sex chromosomes, Spermatogenesis, Science, Biology (General), QH301-705.5 |
الوصف: | Meiosis is precisely regulated by the factors involved in DNA damage response in somatic cells. Among them, phosphorylation of H2AX on Serine 139 (γH2AX) is an essential signal for the silencing of unsynapsed sex chromosomes during male meiosis. However, it remains unknown how adjacent H2AX phosphorylation on Tyrosine 142 (pTyr142) is regulated in meiosis. Here we investigate the meiotic functions of BAZ1B (WSTF), the only known Tyr142 kinase in somatic cells, using mice possessing a conditional deletion of BAZ1B. Although BAZ1B deletion causes ectopic γH2AX signals on synapsed autosomes during the early pachytene stage, BAZ1B is dispensable for fertility and critical events during spermatogenesis. BAZ1B deletion does not alter events on unsynapsed axes and pericentric heterochromatin formation. Furthermore, BAZ1B is dispensable for localization of the ATP-dependent chromatin remodeling protein SMARCA5 (SNF2h) during spermatogenesis despite the complex formation between BAZ1B and SMARCA5, known as the WICH complex, in somatic cells. Notably, pTyr142 is regulated independently of BAZ1B and is dephosphorylated on the sex chromosomes during meiosis in contrast with the presence of adjacent γH2AX. Dephosphorylation of pTyr142 is regulated by MDC1, a binding partner of γH2AX. These results reveal the distinct regulation of two adjacent phosphorylation sites of H2AX during meiosis, and suggest that another kinase mediates Tyr142 phosphorylation. |
نوع الوثيقة: | article |
وصف الملف: | electronic resource |
اللغة: | English |
تدمد: | 2046-6390 |
Relation: | http://bio.biologists.org/content/4/7/873; https://doaj.org/toc/2046-6390 |
DOI: | 10.1242/bio.011734 |
URL الوصول: | https://doaj.org/article/1e636bbe61414bd38cc94120e5ef26d9 |
رقم الأكسشن: | edsdoj.1e636bbe61414bd38cc94120e5ef26d9 |
قاعدة البيانات: | Directory of Open Access Journals |
تدمد: | 20466390 |
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DOI: | 10.1242/bio.011734 |