TRAF interacting protein explained
TRAF-interacting protein is a protein that in humans is encoded by the TRAIP gene.[1] [2]
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.[3]
Interactions
TRAF interacting protein has been shown to interact with FLII,[4] TRAF1 and TRAF2.[1]
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).[5] Intrinsic sources of RS include transcription-replication conflicts and “difficult-to-replicate’’ regions. Extrinsic RS includes exposure to genotoxic agents, depletion of dNTPs, and premature S phase activity which can occur in precancerous cells after oncogene activation. 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.
Further reading
- Beckly JB, Hancock L, Geremia A, Cummings JR, Morris A, Cooney R, Pathan S, Guo C, Jewell DP . 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 . April 2008 . 18200509 . 10.1002/ibd.20365 . 37697301 .
- Regamey A, Hohl D, Liu JW, Roger T, Kogerman P, Toftgard R, Huber M . 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 . December 2003 . 14676304 . 2194148 . 10.1084/jem.20031187 .
- Wilson SA, Brown EC, Kingsman AJ, Kingsman SM . 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 . August 1998 . 9671805 . 147727 . 10.1093/nar/26.15.3460 .
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S . Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library . Gene . 200 . 1-2 . 149–156 . October 1997 . 9373149 . 10.1016/S0378-1119(97)00411-3 .
- Maruyama K, Sugano S . Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides . Gene . 138 . 1-2 . 171–174 . January 1994 . 8125298 . 10.1016/0378-1119(94)90802-8 .
Notes and References
- Lee SY, Lee SY, Choi Y . 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 . April 1997 . 9104814 . 2196258 . 10.1084/jem.185.7.1275 .
- Web site: Entrez Gene: TRAIP TRAF interacting protein.
- Web site: Entrez Gene: TRAIP TRAF interacting protein.
- Wilson SA, Brown EC, Kingsman AJ, Kingsman SM . 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 . August 1998 . 9671805 . 147727 . 10.1093/nar/26.15.3460 .
- Bhowmick R, Hickson ID, Liu Y . Completing genome replication outside of S phase . Molecular Cell . 83 . 20 . 3596–3607 . October 2023 . 37716351 . 10.1016/j.molcel.2023.08.023 . free .