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Human RNF8 Protein expressed in Wheat germ - ABIN1318397
Delker, Zhou, Strikoudis, Stebbins, Papavasiliou: Solubility-based genetic screen identifies RING finger protein 126 as an E3 ligase for activation-induced cytidine deaminase. in Proceedings of the National Academy of Sciences of the United States of America 2013
Show all 2 Pubmed References
Knockdown or conditional knockout of RNF8 or UBC13 (show UBE2N Proteins) in rodent cerebellar granule neurons robustly increases the number of parallel fiber presynaptic boutons and functional parallel fiber/Purkinje cell synapses. In contrast to the role of nuclear RNF8 in proliferating cells, RNF8 operates in the cytoplasm in neurons to suppress synapse differentiation.
RNF8-dependent polyubiquitination is required for the establishment of H3K27 acetylation, a marker of active enhancers, while persistent H2AK119ub inhibits establishment of H3K27 acetylation. Following the deposition of H3K27 acetylation, H3K4 dimethylation is established as an active mark on poised promoters.
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 Proteins)-pathway activation upon loss of Rnf8, suggesting that Rnf8 and p53 (show TP53 Proteins) 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 Proteins) 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 Proteins) 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 Proteins) to generate Ubc13 (show UBE2N Proteins)-dependent Lys63 polyubiquitin (show UBB Proteins) chains that stabilize Tpp1 (show TPP1 Proteins) at telomeres.
the present study described the noncovalent interaction between the E3 ubiquitin ligase (show MUL1 Proteins) RNF8 and SUMO2 (show SUMO2 Proteins)/3 and indicated that this interaction promoted DSB repair.
Data report that RNF8 is overexpressed in highly metastatic breast cell lines and its overexpression can induce EMT (show ITK Proteins) in breast cancer cells. Furthermore, RNF8 is aberrantly expressed in invasive breast cancer and positively correlates with lymph node metastasis.
The present findings indicate that WRAP53beta and RNF8 are rate-limiting factors in the repair of DNA double-strand breaks and raise the possibility that upregulation of WRAP53beta may contribute to genomic stability in and survival of cancer cells.
The study identifies a previously unrecognized role for RNF8 in the negative regulation of NF-kappaB (show NFKB1 Proteins) activation by targeting and deactivating the IKK (show CHUK Proteins) complex.
the role of RNF8-mediated histone H3 (show HIST3H3 Proteins) polyubiquitylation in the regulation of histone H3 (show HIST3H3 Proteins) 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 Proteins) depletion could be attributed to the defective retention of ATM (show ATM Proteins).
In late S/G2 (show STRN3 Proteins) phase, the DNA damage-responsive E3 ligase RNF8 conjugates K63-linked ubiquitin chains to tankyrase 1 (show TNKS Proteins), while in G1 phase such ubiquitin chains are removed by BRISC, an ABRO1 (show FAM175B Proteins)/BRCC36 (show BRCC3 Proteins)-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.
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