TRAF-interacting protein is a protein that in humans is encoded by the TRAIP gene.[6][7]
This gene encodes a protein that contains an N-terminal RING finger motif and a putative coiled-coil domain. A similar murine protein interacts with TNFR-associated factor 1 (TRAF1), TNFR-associated factor 2 (TRAF2), and cylindromatosis. The interaction with TRAF2 inhibits TRAF2-mediated nuclear factor kappa-B, subunit 1 activation that is required for cell activation and protection against apoptosis.[7]
Interactions
TRAF interacting protein has been shown to interact with FLII,[8] TRAF1[6] and TRAF2.[6]
Role in mitotic DNA synthesis
Mitotic DNA synthesis (MiDAS) is thought to be a DNA repair mechanism to salvage DNA that has not finished replication during S phase, which may be due to DNA replication stress (RS).[9] Intrinsic sources of RS include transcription-replication conflicts and “difficult-to-replicate’’ regions.[9] Extrinsic RS includes exposure to genotoxic agents, depletion of dNTPs, and premature S phase activity which can occur in precancerous cells after oncogene activation.[9] Some MiDAS pathways require the TRAIP protein to disassemble the replication complex at the stalled replication fork in cases where RS causes the fork to stall during replication.[9]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000183763 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032586 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Hoffmann S, Smedegaard S, Nakamura K, Mortuza GB, Räschle M, Ibañez de Opakua A, et al. (January 2016). "TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress". The Journal of Cell Biology. 212 (1): 63–75. doi:10.1083/jcb.201506071. PMC 4700480. PMID 26711499.
- ^ a b c Lee SY, Lee SY, Choi Y (April 1997). "TRAF-interacting protein (TRIP): a novel component of the tumor necrosis factor receptor (TNFR)- and CD30-TRAF signaling complexes that inhibits TRAF2-mediated NF-kappaB activation". The Journal of Experimental Medicine. 185 (7): 1275–1285. doi:10.1084/jem.185.7.1275. PMC 2196258. PMID 9104814.
- ^ a b "Entrez Gene: TRAIP TRAF interacting protein".
- ^ Wilson SA, Brown EC, Kingsman AJ, Kingsman SM (August 1998). "TRIP: a novel double stranded RNA binding protein which interacts with the leucine rich repeat of flightless I". Nucleic Acids Research. 26 (15): 3460–3467. doi:10.1093/nar/26.15.3460. PMC 147727. PMID 9671805.
- ^ a b c d Bhowmick R, Hickson ID, Liu Y (October 2023). "Completing genome replication outside of S phase". Molecular Cell. 83 (20): 3596–3607. doi:10.1016/j.molcel.2023.08.023. PMID 37716351.
Further reading
- Beckly JB, Hancock L, Geremia A, Cummings JR, Morris A, Cooney R, et al. (April 2008). "Two-stage candidate gene study of chromosome 3p demonstrates an association between nonsynonymous variants in the MST1R gene and Crohn's disease". Inflammatory Bowel Diseases. 14 (4): 500–507. doi:10.1002/ibd.20365. PMID 18200509. S2CID 37697301.
- Regamey A, Hohl D, Liu JW, Roger T, Kogerman P, Toftgard R, et al. (December 2003). "The tumor suppressor CYLD interacts with TRIP and regulates negatively nuclear factor kappaB activation by tumor necrosis factor". The Journal of Experimental Medicine. 198 (12): 1959–1964. doi:10.1084/jem.20031187. PMC 2194148. PMID 14676304.
- Wilson SA, Brown EC, Kingsman AJ, Kingsman SM (August 1998). "TRIP: a novel double stranded RNA binding protein which interacts with the leucine rich repeat of flightless I". Nucleic Acids Research. 26 (15): 3460–3467. doi:10.1093/nar/26.15.3460. PMC 147727. PMID 9671805.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
External links