NDLI: BCLAF1 is a radiation-induced H2AX-interacting partner involved in Î³H2AX-mediated regulation of apoptosis and DNA repair.

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BCLAF1 is a radiation-induced H2AX-interacting partner involved in Î³H2AX-mediated regulation of apoptosis and DNA repair.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Lee, Y. Y. Yu, Y. B. Gunawardena, H. P. Xie, L. Chen, X.
Description	Country affiliation: United States Author Affiliation: Lee YY ( Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.)
Abstract	H2AX, a histone H2A variant, has a key role in the cellular response to DNA double-strand breaks (DSBs). H2AX senses DSBs through rapid serine 139 phosphorylation, concurrently leading to the formation of phospho-(Î³)H2AX foci with various proteins. However, in the cells with different sensitivity to ionizing radiation (IR)-induced DSBs, still incomplete are those specific proteins selectively recruited by Î³H2AX to decide different cell fates. Because the abundance of Î³H2AX indicates the extent of DSBs, we first identified IR-induced dose-dependent H2AX-interacting partners and found that Bcl-2-associated transcription factor 1 (BCLAF1/Btf) showed enhanced association with Î³H2AX only under high-dose radiation. In acutely irradiated cells, BCLAF1 promoted apoptosis of irreparable cells through disturbing p21-mediated inhibition of Caspase/cyclin E-dependent, mitochondrial-mediated pathways. Meanwhile, BCLAF1 co-localized with Î³H2AX foci in nuclei and stabilized the Ku70/DNA-PKcs complex therein, facilitating non-homologous end joining (NHEJ)-based DSB repair in surviving cells. In tumor cells, BCLAF1 was intrinsically suppressed, leading to formation of anti-apoptotic Ku70-Bax complexes and disruption of Ku70/DNA-PKcs complexes, all of which contribute to tumor-associated apoptotic resistance and cell survival with defective NHEJ DNA repair. For the first time, our studies reveal that, based on the extent of DNA damage, BCLAF1 is involved in the Î³H2AX-mediated regulation of apoptosis and DNA repair, and is a Î³H2AX-interacting tumor suppressor.
File Format	HTM / HTML
e-ISSN	20414889
DOI	10.1038/cddis.2012.76
Journal	Cell Death and Disease
Volume Number	3
Language	English
Publisher	Nature Publishing Group
Publisher Date	2012-07-26
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Research Support, N.i.h., Extramural Dna Repair Dna-binding Proteins Repressor Proteins Dna Breaks, Double-stranded Antagonists & Inhibitors Mitochondria Antigens, Nuclear Hek293 Cells Histones G1 Phase Cell Cycle Checkpoints Bcl-2-associated X Protein Genetics Cyclin E Radiation, Ionizing Research Support, U.s. Gov't, Non-p.h.s. Cell Line Rna, Small Interfering Computational Biology Metabolism Rna Interference Discipline Cell Biology Radiation Effects Caspases Tumor Suppressor Proteins Cyclin-dependent Kinase Inhibitor P21 Apoptosis
Content Type	Text
Resource Type	Article

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