Study on RF8: Functions and Potential Therapeutics (G9025)

Target Name: RNF8

NCBI ID: G9025

RNF8

Study on RF8: Functions and Potential Therapeutics

Ring finger protein 8 (RF8) is a protein that is expressed in nearly all eukaryotic cells, including mammals, birds, fish, and insects. However, the function and role of RF8 in cells are still not completely clear. In recent years, researchers have discovered that RF8 plays an important role in many biological processes, including cell proliferation, differentiation, and tumor formation. In addition, RF8 is also associated with many diseases and drug targets. Therefore, RF8 has become a research subject that has attracted much attention.

biological function

RF8 plays an important role in many biological processes. For example, RF8 is a key component in the assembly and stabilization of spindle microtubules during the cell cycle. During mitosis, RF8 binds to tubulin, helping microtubules form the correct shape and providing support on spindle fibers. In addition, RF8 is also related to cell wall formation after mitosis.

RF8 also plays an important role in cell differentiation and tumor formation. During the differentiation process, RF8 can help cells maintain stable shape and structure, thereby ensuring correct function. In addition, RF8 is also closely related to tumor occurrence and development. Studies have shown that the expression level of RF8 is positively correlated with tumor invasion and metastasis.

drug target

RF8 is an important drug target and has become the target of many drug studies. For example, researchers have found that inhibiting RF8 can inhibit the growth and spread of tumor cells. In addition, RF8 has also been used as a target for many drugs, including cancer treatment drugs and immunomodulatory drugs.

molecular mechanism

The biological functions and effects of RF8 are achieved in various ways. For example, RF8 can regulate microtubule assembly and function through phosphorylation modification. In addition, RF8 can regulate key steps in the cell cycle by binding to other proteins.

The pathological significance of RF8 also deserves attention. Studies have shown that the expression level of RF8 is closely related to the occurrence and development of many diseases, including cancer, neurodegenerative diseases, immune deficiency diseases, etc. Therefore, studying the pathological significance of RF8 is of great significance for understanding the mechanism of disease occurrence and development.

in conclusion

RF8 is a protein that plays an important role in biological processes. In recent years, researchers have found that RF8 is also related to many diseases and drug targets. In addition, the molecular mechanism of RF8 and its relationship with diseases have also attracted much attention. Therefore, future research will continue to further study the role of RF8 in biological processes, with a view to providing new ideas and targets for the treatment of many diseases.

Protein Name: Ring Finger Protein 8

Functions: E3 ubiquitin-protein ligase that plays a key role in DNA damage signaling via 2 distinct roles: by mediating the 'Lys-63'-linked ubiquitination of histones H2A and H2AX and promoting the recruitment of DNA repair proteins at double-strand breaks (DSBs) sites, and by catalyzing 'Lys-48'-linked ubiquitination to remove target proteins from DNA damage sites. Following DNA DSBs, it is recruited to the sites of damage by ATM-phosphorylated MDC1 and catalyzes the 'Lys-63'-linked ubiquitination of histones H2A and H2AX, thereby promoting the formation of TP53BP1 and BRCA1 ionizing radiation-induced foci (IRIF). Also controls the recruitment of UIMC1-BRCC3 (RAP80-BRCC36) and PAXIP1/PTIP to DNA damage sites. Also recruited at DNA interstrand cross-links (ICLs) sites and catalyzes 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Promotes the formation of 'Lys-63'-linked polyubiquitin chains via interactions with the specific ubiquitin-conjugating UBE2N/UBC13 and ubiquitinates non-histone substrates such as PCNA. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation. Also catalyzes the formation of 'Lys-48'-linked polyubiquitin chains via interaction with the ubiquitin-conjugating UBE2L6/UBCH8, leading to degradation of substrate proteins such as CHEK2, JMJD2A/KDM4A and KU80/XRCC5: it is still unclear how the preference toward 'Lys-48'- versus 'Lys-63'-linked ubiquitination is regulated but it could be due to RNF8 ability to interact with specific E2 specific ligases. For instance, interaction with phosphorylated HERC2 promotes the association between RNF8 and UBE2N/UBC13 and favors the specific formation of 'Lys-63'-linked ubiquitin chains. Promotes non-homologous end joining (NHEJ) by promoting the 'Lys-48'-linked ubiquitination and degradation the of KU80/XRCC5. Following DNA damage, mediates the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF168, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites (PubMed:11322894, PubMed:14981089, PubMed:17724460, PubMed:18001824, PubMed:18001825, PubMed:18006705, PubMed:18077395, PubMed:18337245, PubMed:18948756, PubMed:19015238, PubMed:19124460, PubMed:19202061, PubMed:19203578, PubMed:19203579, PubMed:20550933, PubMed:21558560, PubMed:21857671, PubMed:21911360, PubMed:22266820, PubMed:22373579, PubMed:22531782, PubMed:22705371, PubMed:22865450, PubMed:22980979). Following DNA damage, mediates the ubiquitination and degradation of POLD4/p12, a subunit of DNA polymerase delta. In the absence of POLD4, DNA polymerase delta complex exhibits higher proofreading activity (PubMed:23233665). In addition to its function in damage signaling, also plays a role in higher-order chromatin structure by mediating extensive chromatin decondensation. Involved in the activation of ATM by promoting histone H2B ubiquitination, which indirectly triggers histone H4 'Lys-16' acetylation (H4K16ac), establishing a chromatin environment that promotes efficient activation of ATM kinase. Required in the testis, where it plays a role in the replacement of histones during spermatogenesis. At uncapped telomeres, promotes the joining of deprotected chromosome ends by inducing H2A ubiquitination and TP53BP1 recruitment, suggesting that it may enhance cancer development by aggravating telomere-induced genome instability in case of telomeric crisis. Promotes the assembly of RAD51 at DNA DSBs in the absence of BRCA1 and TP53BP1 Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. May be required for proper exit from mitosis after spindle checkpoint activation and may regulate cytokinesis. May play a role in the regulation of RXRA-mediated transcriptional activity. Not involved in RXRA ubiquitination by UBE2E2 (PubMed:11322894, PubMed:14981089, PubMed:17724460, PubMed:18001824, PubMed:18001825, PubMed:18006705, PubMed:18077395, PubMed:18337245, PubMed:18948756, PubMed:19015238, PubMed:19124460, PubMed:19202061, PubMed:19203578, PubMed:19203579, PubMed:20550933, PubMed:21558560, PubMed:21857671, PubMed:21911360, PubMed:22266820, PubMed:22373579, PubMed:22531782, PubMed:22705371, PubMed:22865450, PubMed:22980979)

The "RNF8 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about RNF8 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
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•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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