RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins (Q24300411)

positive regulation of DNA repair

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

1 reference

Jiri Bartek

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Jiří Lukáš

Helene Faustrup Kildegaard

object named as

Jiri Lukas

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Claudia Lukas

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Simon Bekker-Jensen

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1 reference

ORCID Public Data File 2021

author name string

Niels Mailand

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Helene Faustrup

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Fredrik Melander

The RING finger protein RNF8 recruits UBC13 for lysine 63-based self polyubiquitylation

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language of work or name

English

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publication date

30 November 2007

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published in

Cell

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volume

131

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issue

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page(s)

887-900

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cites work

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MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks

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Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair

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Chromatin modifications and their function

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RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly

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Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation

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The Mre11 complex and the metabolism of chromosome breaks: the importance of communicating and holding things together

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H2AX: the histone guardian of the genome

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gammaH2AX and MDC1: anchoring the DNA-damage-response machinery to broken chromosomes

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MDC1 maintains genomic stability by participating in the amplification of ATM-dependent DNA damage signals

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Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage

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Destruction of Claspin by SCFbetaTrCP restrains Chk1 activation and facilitates recovery from genotoxic stress

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MDC1 is required for the intra-S-phase DNA damage checkpoint

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MDC1 is a mediator of the mammalian DNA damage checkpoint

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Role of histone H2A ubiquitination in Polycomb silencing

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Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks

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Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA damage

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ATM- and cell cycle-dependent regulation of ATR in response to DNA double-strand breaks

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Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks

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Distinct spatiotemporal dynamics of mammalian checkpoint regulators induced by DNA damage

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Mdc1 couples DNA double-strand break recognition by Nbs1 with its H2AX-dependent chromatin retention

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A conserved pathway to activate BRCA1-dependent ubiquitylation at DNA damage sites.

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Cellular functions of the BRCA tumour-suppressor proteins

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N-Terminally extended human ubiquitin-conjugating enzymes (E2s) mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8

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53BP1 and p53 synergize to suppress genomic instability and lymphomagenesis.

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Direct DNA binding by Brca1

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Mediator of DNA damage checkpoint protein 1 regulates BRCA1 localization and phosphorylation in DNA damage checkpoint control

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Dynamic assembly and sustained retention of 53BP1 at the sites of DNA damage are controlled by Mdc1/NFBD1

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Changes in chromatin structure and mobility in living cells at sites of DNA double-strand breaks

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BRCA1 : BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair

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DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A

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ATR and ATRIP: partners in checkpoint signaling

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Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response

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RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites

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Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response

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ATM activation and its recruitment to damaged DNA require binding to the C terminus of Nbs1.

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53BP1 cooperates with p53 and functions as a haploinsufficient tumor suppressor in mice

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Silencing of unpaired chromatin and histone H2A ubiquitination in mammalian meiosis

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The ubiquitin-interacting motif containing protein RAP80 interacts with BRCA1 and functions in DNA damage repair response

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