Neddylation Promotes Ubiquitylation and Release of Ku from DNA-Damage Sites
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چکیده
منابع مشابه
Neddylation Promotes Ubiquitylation and Release of Ku from DNA-Damage Sites
The activities of many DNA-repair proteins are controlled through reversible covalent modification by ubiquitin and ubiquitin-like molecules. Nonhomologous end-joining (NHEJ) is the predominant DNA double-strand break (DSB) repair pathway in mammalian cells and is initiated by DSB ends being recognized by the Ku70/Ku80 (Ku) heterodimer. By using MLN4924, an anti-cancer drug in clinical trials t...
متن کاملUbiquitylation, neddylation and the DNA damage response
Failure of accurate DNA damage sensing and repair mechanisms manifests as a variety of human diseases, including neurodegenerative disorders, immunodeficiency, infertility and cancer. The accuracy and efficiency of DNA damage detection and repair, collectively termed the DNA damage response (DDR), requires the recruitment and subsequent post-translational modification (PTM) of a complex network...
متن کاملRNF168-mediated H2A neddylation antagonizes ubiquitylation of H2A and regulates DNA damage repair.
NEDD8 is an important regulatory factor in many biological processes. However, the substrates for neddylation, and the relationship between the ubiquitin and NEDD8 pathways remain largely unknown. Here, we show that NEDD8 is covalently conjugated to histone 2A (H2A), and that neddylation of H2A antagonizes its ubiquitylation. NEDD8 suppresses ubiquitylation of H2A, and a decreased level of free...
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Involvement of the ubiquitin system in DNA repair and DNA damage signaling has been extensively studied during the last decade. Dynamic modification of proteins with ubiquitin after DNA damage has been shown to play important roles in virtually all DNA repair pathways [1]. In this regard, protein ubiquitylation has most frequently been associated with the recruitment of DNA repair factors – man...
متن کاملRapid PIKK-Dependent Release of Chk1 from Chromatin Promotes the DNA-Damage Checkpoint Response
BACKGROUND Checkpoint signaling pathways are of crucial importance for the maintenance of genomic integrity. Within these pathways, the effector kinase Chk1 plays a central role in mediating cell-cycle arrest in response to DNA damage, and it does so by phosphorylating key cell-cycle regulators. RESULTS By investigating the subcellular distribution of Chk1 by cell fractionation, we observed t...
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ژورنال
عنوان ژورنال: Cell Reports
سال: 2015
ISSN: 2211-1247
DOI: 10.1016/j.celrep.2015.03.058