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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Ring finger protein 168

This gene encodes an E3 ubiquitin ligase protein that contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-DNA and protein-protein interactions. The protein is involved in DNA double-strand break (DSB) repair. Mutations in this gene result in Riddle syndrome. [provided by RefSeq, Sep 2011] (from NCBI)
Top mentioned proteins: Ubiquitin, RNF8, 53BP1, Iris, Histone
Papers on RNF168
Hypermethylation of genes in testicular embryonal carcinomas.
Chan et al., Hong Kong, Hong Kong. In Br J Cancer, Feb 2016
RNF168 and USP13 are potential tumour suppressors.
USP11 Is a Negative Regulator to γH2AX Ubiquitylation by RNF8/RNF168.
Zhao et al., Beijing, China. In J Biol Chem, Feb 2016
Here, we found that RNF8/RNF168 ubiquitylates γH2AX.
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.
Ubiquitin-Activated Interaction Traps (UBAITs) identify E3 ligase binding partners.
Huibregtse et al., Austin, United States. In Embo Rep, Dec 2015
We designed UBAITs for both HECT (Rsp5, Itch) and RING (Psh1, RNF126, RNF168) E3s.
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.
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.
Ataxia telangiectasia: more variation at clinical and cellular levels.
Byrd et al., Birmingham, United Kingdom. In Clin Genet, Mar 2015
There is also locus heterogeneity because mutation of the MRE11 gene can cause an obvious A-T like disorder both clinically and also at the cellular level and mutation of the RNF168 gene results in a much milder clinical phenotype, neurologically, with the major clinical feature being an immunological defect.
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.
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark.
Durocher et al., Toronto, Canada. In Nature, 2013
To accomplish its function in DNA repair, 53BP1 accumulates at DSB sites downstream of the RNF168 ubiquitin ligase.
A two-step mechanism for TRF2-mediated chromosome-end protection.
Denchi et al., Los Angeles, United States. In Nature, 2013
This novel modulation of the DDR at telomeres occurs at the level of the E3 ubiquitin ligase RNF168 (ref.
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 is initiated by two E3 ligases, RNF8 and RNF168, targeting histone H2A and H2AX. Study shows that ubiquitin chains per se are insufficient for signaling, but RNF168 target ubiquitination is required for DDR.
Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks.
Durocher et al., Toronto, Canada. In Mol Cell, 2012
RNF168, its paralog RNF169, RAD18, and the BRCA1-interacting RAP80 protein accumulate at DNA double strand break sites through the use of bipartite modules composed of ubiquitin binding domains.
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 novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase.
Penengo et al., Novara, Italy. In Cell Cycle, 2012
Inactivation of K13 and K15 reduces RNF168- dependent ubiquitination of histones H2As, while inactivation of both N- and C-terminal sites completely abolishes histone ubiquitination.
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.
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.
DNA-damage response and repair activities at uncapped telomeres depend on RNF8.
Jacobs et al., Amsterdam, Netherlands. In Nat Cell Biol, 2011
Data show that depletion of RNF8, as well as of the E3 ligase RNF168, reduces telomere-induced genome instability.
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