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Ring finger protein 8

The protein encoded by this gene contains a RING finger motif and an FHA domain. This protein has been shown to interact with several class II ubiquitin-conjugating enzymes (E2), including UBE2E1/UBCH6, UBE2E2, and UBE2E3, and may act as an ubiquitin ligase (E3) in the ubiquitination of certain nuclear proteins. This protein is also known to play a role in the DNA damage response and depletion of this protein causes cell growth inhibition and cell cycle arrest. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2012] (from NCBI)
Top mentioned proteins: Ubiquitin, RNF168, 53BP1, Iris, H2A
Papers on RNF8
Adenovirus-mediated downregulation of the ubiquitin ligase RNF8 sensitizes bladder cancer to radiotherapy.
Wang et al., Lanzhou, China. In Oncotarget, Feb 2016
UNASSIGNED: The ubiquitin ligase RNF8 promotes the DNA damage response (DDR).
Lanatoside C suppressed colorectal cancer cell growth by inducing mitochondrial dysfunction and increased radiation sensitivity by impairing DNA damage repair.
Jeong et al., Seoul, South Korea. In Oncotarget, Feb 2016
This may have been due to defects in the RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A that increases 53BP1 recruitment to DNA damage sites.
Identification of RNF168 as a PML nuclear body regulator.
Frappier et al., Toronto, Canada. In J Cell Sci, Jan 2016
We screened an shRNA library targeting ubiquitin pathway proteins for effects on PML NBs and identified RNF8 and RNF168 DNA damage response proteins as negative regulators of PML NBs.
The Ku70/80 ring in Non-Homologous End-Joining: easy to slip on, hard to remove.
Keijzers et al., Copenhagen, Denmark. In Front Biosci, Dec 2015
Recent studies suggest that Ku80 is conjugated to lysine48-linked ubiquitin chains by the Skp1-Cullin-F-box (SCF) complex and/or the RING finger protein 8 (RNF8) ubiquitin-protein ligases, followed by rapid proteasomal degradation.
Histone H1 couples initiation and amplification of ubiquitin signalling after DNA damage.
Mailand et al., Copenhagen, Denmark. In Nature, Dec 2015
This depends on the sequential actions of the E3 ubiquitin ligases RNF8 and RNF168 (refs 1-6), and UBC13 (also known as UBE2N), an E2 ubiquitin-conjugating enzyme that specifically generates K63-linked ubiquitin chains.
The proximity ligation assay reveals that at DNA double-strand breaks WRAP53β associates with γH2AX and controls interactions between RNF8 and MDC1.
Farnebo et al., Cocos Islands. In Nucleus, Oct 2015
Moreover, formation of complexes between MDC1 and both its partners RNF8 and phosphorylated ATM was visualized.
MAD2L2 controls DNA repair at telomeres and DNA breaks by inhibiting 5' end resection.
Jacobs et al., Amsterdam, Netherlands. In Nature, Jun 2015
These activities of MAD2L2 depend on ATM kinase activity, RNF8, RNF168, 53BP1 and RIF1, but not on PTIP, REV1 and REV3, the latter two acting with MAD2L2 in translesion synthesis.
REV7 counteracts DNA double-strand break resection and affects PARP inhibition.
Rottenberg et al., Amsterdam, Netherlands. In Nature, Jun 2015
REV7 is recruited to DSBs in a manner dependent on the H2AX-MDC1-RNF8-RNF168-53BP1 chromatin pathway, and seems to block HR and promote end joining in addition to its regulatory role in DNA damage tolerance.
Fine-tuning the ubiquitin code at DNA double-strand breaks: deubiquitinating enzymes at work.
Citterio, Amsterdam, Netherlands. In Front Genet, 2014
In particular, the DSB response critically relies on active ubiquitination by the RNF8 and RNF168 ub ligases at the chromatin, which is essential for proper DSB signaling and repair.
Mitosis inhibits DNA double-strand break repair to guard against telomere fusions.
Durocher et al., Toronto, Canada. In Science, 2014
Mitotic kinases phosphorylate the E3 ubiquitin ligase RNF8 and the nonhomologous end joining factor 53BP1 to inhibit their recruitment to DSB-flanking chromatin.
RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA damage signaling.
Sixma et al., Amsterdam, Netherlands. In Cell, 2012
Ubiquitin-dependent signaling during the DNA damage response (DDR) to double-strand breaks (DSBs) is initiated by two E3 ligases, RNF8 and RNF168, targeting histone H2A and H2AX.
A ubiquitin-binding protein, FAAP20, links RNF8-mediated ubiquitination to the Fanconi anemia DNA repair network.
Wang et al., Baltimore, United States. In Mol Cell, 2012
Data indicate that RNF8 and FAAP20 (C1orf86) are needed for efficient Fanconi anemia group D2 protein FANCD2 monoubiquitination.
Molecular insights into the function of RING finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation.
Glover et al., Edmonton, Canada. In J Biol Chem, 2012
Data show RING finger (RNF) E3 ubiquitin ligase RNF8 dimerizes and binds to E2 ubiquitin-conjugating complex Ubc13/Mms2 with formation of Lys-63 ubiquitin chains, whereas the RNF168 RING domain is a monomer and does not catalyze Lys-6 ubiquitylation.
A new non-catalytic role for ubiquitin ligase RNF8 in unfolding higher-order chromatin structure.
Dantuma et al., Stockholm, Sweden. In Embo J, 2012
A new mechanism of chromatin remodelling-assisted ubiquitylation was shown, which involves cooperation between CHD4 and RNF8 to create a local chromatin environment permissive to the assembly of checkpoint and repair machineries at DNA lesions.
Close encounters of the RNF8th kind: when chromatin meets DNA repair.
van Attikum et al., Leiden, Netherlands. In Curr Opin Cell Biol, 2012
Emerging evidence suggests that the histone ubiquitin ligases RNF8/RNF168 act in concert with ATP-dependent chromatin remodelling enzymes to orchestrate the signalling and repair of DNA lesions in specific chromatin topologies.
DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger.
Mailand et al., Copenhagen, Denmark. In J Cell Biol, 2012
In response to double-strand breaks, both HERC2 and RNF168 were specifically modified with SUMO1 at double-strand break sites in a manner dependent on the SUMO E3 ligase PIAS4.
Viral E3 ubiquitin ligase-mediated degradation of a cellular E3: viral mimicry of a cellular phosphorylation mark targets the RNF8 FHA domain.
Weitzman et al., Los Angeles, United States. In Mol Cell, 2012
By mimicking a cellular phosphosite, ICP0 binds RNF8 via the RNF8 forkhead associated (FHA) domain. Phosphorylation of ICP0 T67 by CK1 recruits RNF8 for degradation and thereby promotes viral transcription
Fusing telomeres with RNF8.
Jacobs, Amsterdam, Netherlands. In Nucleus, 2012
DNA repair activities at DNA double-strand breaks (DSBs) are under control of regulatory ubiquitylation events governed by the RNF8 and RNF168 ubiquitin-ligases.
The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks.
Mailand et al., Copenhagen, Denmark. In Febs Lett, 2011
Studies indicate that Non-proteolytic ubiquitylation of chromatin surrounding DSBs, mediated by the RNF8/RNF168 ubiquitin ligase cascade, has emerged as a key mechanism for restoration of genome integrity.
RNF8-dependent histone ubiquitination during DNA damage response and spermatogenesis.
Yu et al., Ann Arbor, United States. In Acta Biochim Biophys Sin (shanghai), 2011
Recently, ubiquitination of histones was observed during the DNA damage response (DDR), and this modification is controlled by really interesting new gene (RING) domain E3 ligase, RNF8.
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