DNA Damage Detection by 53BP1: Relationship to Species Longevity
نویسندگان
چکیده
منابع مشابه
PTIP regulates 53BP1 and SMC1 at the DNA damage sites.
Although PTIP is implicated in the DNA damage response, through interactions with 53BP1, the function of PTIP in the DNA damage response remain elusive. Here, we show that RNF8 controls DNA damage-induced nuclear foci formation of PTIP, which in turn regulates 53BP1 localization to the DNA damage sites. In addition, SMC1, a substrate of ATM, could not be phosphorylated at the DNA damage sites i...
متن کاملTopBP1 functions with 53BP1 in the G1 DNA damage checkpoint.
TopBP1 is a checkpoint protein that colocalizes with ATR at sites of DNA replication stress. In this study, we show that TopBP1 also colocalizes with 53BP1 at sites of DNA double-strand breaks (DSBs), but only in the G1-phase of the cell cycle. Recruitment of TopBP1 to sites of DNA replication stress was dependent on BRCT domains 1-2 and 7-8, whereas recruitment to sites of DNA DSBs was depende...
متن کاملHistone deacetylase 4 interacts with 53BP1 to mediate the DNA damage response
Anumber of proteins are recruited to nuclear foci upon exposure to double-strand DNA damage, including 53BP1 and Rad51, but the precise role of these DNA damage-induced foci remain unclear. Here we show in a variety of human cell lines that histone deacetylase (HDAC) 4 is recruited to foci with kinetics similar to, and colocalizes with, 53BP1 after exposure to agents causing double-stranded DNA...
متن کاملRIDDLE immunodeficiency syndrome is linked to defects in 53BP1-mediated DNA damage signaling.
Cellular DNA double-strand break-repair pathways have evolved to protect the integrity of the genome from a continual barrage of potentially detrimental insults. Inherited mutations in genes that control this process result in an inability to properly repair DNA damage, ultimately leading to developmental defects and also cancer predisposition. Here, we describe a patient with a previously unde...
متن کاملUbiquitin-H2AX fusions render 53BP1 recruitment to DNA damage sites independent of RNF8 or RNF168
The mammalian E3 ubiquitin ligases RNF8 and RNF168 facilitate recruitment of the DNA damage response protein 53BP1 to sites of DNA double-strand breaks (DSBs). The mechanism involves recruitment of RNF8, followed by recruitment of RNF168, which ubiquitinates histones H2A/H2AX on K15. 53BP1 then binds to nucleosomes at sites of DNA DSBs by recognizing, in addition to methyl marks, histone H2A/H2...
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ژورنال
عنوان ژورنال: The Journals of Gerontology Series A: Biological Sciences and Medical Sciences
سال: 2016
ISSN: 1079-5006,1758-535X
DOI: 10.1093/gerona/glw170