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RNF8-promoted Twist ubiquitination is required for Twist localization to the nucleus for subsequent epithelial-mesenchymal transition and cancer stem cells functions, thereby conferring chemoresistance.
Structure-guided separation-of-function mutations show that the RNF8 E2 stimulating activity is essential for DSB signaling in mammalian cells and is necessary for downstream recruitment of 53BP1 and BRCA1.
RNF8(-/-) mice exhibit neuronal degeneration and reactive astrocytosis. Neurons from RNF8(-/-) mice appear to be more susceptible to X-ray-induced DNA damage
Altogether, the data in this study highlight the importance of p53 (show TP53 ELISA Kits)-pathway activation upon loss of Rnf8, suggesting that Rnf8 and p53 (show TP53 ELISA Kits) functionally interact to protect against genomic instability and tumorigenesis.
The identification of RNF8 allows new insights into the integration of the control of p12 (show CDK2AP1 ELISA Kits) degradation by different DNA damage signaling pathways.
RNF8-dependent ubiquitination of histone H2A during meiosis establishes active epigenetic modifications, including dimethylation of H3K4 on the sex chromosomes
A new mechanism of chromatin remodelling-assisted ubiquitylation was shown, which involves cooperation between CHD4 (show CHD4 ELISA Kits) and RNF8 to create a local chromatin environment permissive to the assembly of checkpoint and repair machineries at DNA lesions.
Rnf8 physically interacts with Tpp1 (show TPP1 ELISA Kits) to generate Ubc13 (show UBE2N ELISA Kits)-dependent Lys63 polyubiquitin (show UBB ELISA Kits) chains that stabilize Tpp1 (show TPP1 ELISA Kits) at telomeres.
RNF8 and Chfr, function together to activate ATM (show ATM ELISA Kits) and maintain genomic stability in vivo.
53BP1 (show TP53BP1 ELISA Kits) protein binds to Rnf8, suggesting DNA damage involves RNF8 dependent ubiquitylation, which allows its accumulation at damaged chromatin.
The study identifies a previously unrecognized role for RNF8 in the negative regulation of NF-kappaB (show NFKB1 ELISA Kits) activation by targeting and deactivating the IKK (show CHUK ELISA Kits) complex.
the role of RNF8-mediated histone H3 (show HIST3H3 ELISA Kits) polyubiquitylation in the regulation of histone H3 (show HIST3H3 ELISA Kits) stability and chromatin modification, is reported.
RNF8- and Ube2S-dependent Lys11-linkage ubiquitin conjugation plays an important role in regulating DNA damage-induced transcriptional silencing, distinct from the role of Lys63-linkage ubiquitin in the recruitment of DNA damage repair proteins 53BP1 and BRCA1.
The attenuated DNA damage localization of RNF8 resulting from INT6 (show EIF3E ELISA Kits) depletion could be attributed to the defective retention of ATM (show ATM ELISA Kits).
In late S/G2 (show STRN3 ELISA Kits) phase, the DNA damage-responsive E3 ligase RNF8 conjugates K63-linked ubiquitin chains to tankyrase 1 (show TNKS ELISA Kits), while in G1 phase such ubiquitin chains are removed by BRISC, an ABRO1 (show FAM175B ELISA Kits)/BRCC36 (show BRCC3 ELISA Kits)-containing deubiquitinase complex.
Findings indicate direct interaction of dual-specificity tyrosine phosphorylation-regulated kinase 2 (DYRK2) with ring finger protein (C3HC4 type) 8 (RNF8) in regulating response to DNA damage.
High RNF8 expression is associated with bladder cancer.
The interaction of MDC1 (show MDC1 ELISA Kits) with RNF8, but not with ATM (show ATM ELISA Kits) requires WRAP53beta, suggesting that WRAP53beta facilitates the former interaction without altering phosphorylation of MDC1 (show MDC1 ELISA Kits) by ATM (show ATM ELISA Kits).
These findings elucidate deeply and extensively the mechanism of RNF8/RNF168 (show RNF168 ELISA Kits) and USP11 (show USP11 ELISA Kits) to maintain the proper status of ubiquitylation gammaH2AX (show H2AFX ELISA Kits) to repair double strand breaks.
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.
E3 ubiquitin-protein ligase RNF8
, ActA binding protein 2
, actA-interacting protein 37
, C3HC4-type zinc finger protein
, UBC13/UEV-interacting ring finger protein
, ring finger protein (C3HC4 type) 8
, E3 ubiquitin-protein ligase RNF8 A
, E3 ubiquitin-protein ligase RNF8-A
, RING finger protein 8 A
, RING finger protein 8-A