Critical Role of Monoubiquitination of Histone H2AX Protein in Histone H2AX Phosphorylation and DNA Damage Response
نویسندگان
چکیده
منابع مشابه
Critical role of lysine 134 methylation on histone H2AX for γ-H2AX production and DNA repair
The presence of phosphorylated histone H2AX (γ-H2AX) is associated with the local activation of DNA-damage repair pathways. Although γ-H2AX deregulation in cancer has previously been reported, the molecular mechanism involved and its relationship with other histone modifications remain largely unknown. Here we find that the histone methyltransferase SUV39H2 methylates histone H2AX on lysine 134...
متن کاملHistone H2AX in DNA repair
In eucaryotic cells, DNA is bound to various proteins and forms a complex nucleoprotein structure called chromatin. Indispensable and ubiquitous chromatin components are histones, small proteins of highly conserved primary structure. Two molecules of each H2A, H2B, H3 and H4 type, form the nucleosomal core around which a 146 base pair (bp) stretch of DNA is wrapped. Histone H1 is bound to about...
متن کاملMST1 promotes apoptosis through phosphorylation of histone H2AX.
MST1 (mammalian STE20-like kinase 1) is a serine/threonine kinase that is cleaved and activated by caspases during apoptosis. Overexpression of MST1 induces apoptotic morphological changes such as chromatin condensation, but the mechanism is not clear. Here we show that MST1 induces apoptotic chromatin condensation through its phosphorylation of histone H2AX at Ser-139. During etoposide-induced...
متن کاملMicroRNA-138 modulates DNA damage response by repressing histone H2AX expression.
Precise regulation of DNA damage response is crucial for cellular survival after DNA damage, and its abrogation often results in genomic instability in cancer. Phosphorylated histone H2AX (γH2AX) forms nuclear foci at sites of DNA damage and facilitates DNA damage response and repair. MicroRNAs (miRNA) are short, nonprotein-encoding RNA molecules, which posttranscriptionally regulate gene expre...
متن کاملA critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage
BACKGROUND The response of eukaryotic cells to double-strand breaks in genomic DNA includes the sequestration of many factors into nuclear foci. Recently it has been reported that a member of the histone H2A family, H2AX, becomes extensively phosphorylated within 1-3 minutes of DNA damage and forms foci at break sites. RESULTS In this work, we examine the role of H2AX phosphorylation in focus...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2011
ISSN: 0021-9258
DOI: 10.1074/jbc.m111.257469