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The neurodevelopmental and facial phenotype in individuals with a TRIP12 variant.
Aerden M, Denommé-Pichon AS, Bonneau D, Bruel AL, Delanne J, Gérard B, Mazel B, Philippe C, Pinson L, Prouteau C, Putoux A, Tran Mau-Them F, Viora-Dupont É, Vitobello A, Ziegler A, Piton A, Isidor B, Francannet C, Maillard PY, Julia S, Philippe A, Schaefer E, Koene S, Ruivenkamp C, Hoffer M, Legius E, Theunis M, Keren B, Buratti J, Charles P, Courtin T, Misra-Isrie M, van Haelst M, Waisfisz Q, Wieczorek D, Schmetz A, Herget T, Kortüm F, Lisfeld J, Debray FG, Bramswig NC, Atallah I, Fodstad H, Jouret G, Almoguera B, Tahsin-Swafiri S, Santos-Simarro F, Palomares-Bralo M, López-González V, Kibaek M, Tørring PM, Renieri A, Bruno LP, Õunap K, Wojcik M, Hsieh TC, Krawitz P, Van Esch H. Aerden M, et al. Eur J Hum Genet. 2023 Apr;31(4):461-468. doi: 10.1038/s41431-023-01307-x. Epub 2023 Feb 7. Eur J Hum Genet. 2023. PMID: 36747006 Free PMC article.
Only a limited number of cases have been reported to date. We aimed to further delineate the TRIP12-associated phenotype and objectify characteristic facial traits through GestaltMatcher image analysis based on deep-learning algorithms in order to establish a TRIP12 …
Only a limited number of cases have been reported to date. We aimed to further delineate the TRIP12-associated phenotype and objectif …
The TRIP12 E3 ligase induces SWI/SNF component BRG1-beta-catenin interaction to promote Wnt signaling.
Kassel S, Yuan K, Bunnag N, Neitzel LR, Lu W, Schwarzkopf A, Maines B, Loberg MA, Xu G, Adams A, McCray AD, Cho A, Rockouski M, Orton G, Goldsmith L, Aronno MMA, Spencer ZT, Khan OM, Ye F, Williams C, Lebensohn AM, Rohatgi R, Wang X, Weiss VL, Hong CC, Kettenbach AN, Robbins DJ, Ahmed Y, Lee E. Kassel S, et al. Nat Commun. 2025 Jun 5;16(1):5248. doi: 10.1038/s41467-025-60535-5. Nat Commun. 2025. PMID: 40473626 Free PMC article.
Genetic epistasis experiments place TRIP12 activity downstream of the beta-catenin destruction complex. TRIP12 interacts with and ubiquitylates BRG1, and BRG1 depletion blocks TRIP12-mediated Wnt pathway activation. TRIP12 promotes BRG1 binding to beta …
Genetic epistasis experiments place TRIP12 activity downstream of the beta-catenin destruction complex. TRIP12 interacts with …
TRIP12 structures reveal HECT E3 formation of K29 linkages and branched ubiquitin chains.
Maiwald SA, Schneider LA, Vollrath R, Liwocha J, Maletic MD, Swatek KN, Mulder MPC, Schulman BA. Maiwald SA, et al. Nat Struct Mol Biol. 2025 Sep;32(9):1766-1775. doi: 10.1038/s41594-025-01561-1. Epub 2025 May 26. Nat Struct Mol Biol. 2025. PMID: 40419785 Free PMC article.
Here we utilize biochemistry, chemistry, and cryo-EM to define the catalytic architecture producing K29 linkages and K29/K48 branches for the human HECT E3 TRIP12. TRIP12 resembles a pincer. One pincer side comprises tandem ubiquitin-binding domains, engaging the pr …
Here we utilize biochemistry, chemistry, and cryo-EM to define the catalytic architecture producing K29 linkages and K29/K48 branches for th …
E3 Ubiquitin Ligase TRIP12: Regulation, Structure, and Physiopathological Functions.
Brunet M, Vargas C, Larrieu D, Torrisani J, Dufresne M. Brunet M, et al. Int J Mol Sci. 2020 Nov 12;21(22):8515. doi: 10.3390/ijms21228515. Int J Mol Sci. 2020. PMID: 33198194 Free PMC article. Review.
First described as an interactor of the thyroid hormone receptor, TRIP12's biological importance was revealed by the embryonic lethality of a murine model bearing an inactivating mutation in the TRIP12 gene. ...Moreover, alterations of TRIP12 expression have …
First described as an interactor of the thyroid hormone receptor, TRIP12's biological importance was revealed by the embryonic lethal …
TRIP12 ubiquitination of glucocerebrosidase contributes to neurodegeneration in Parkinson's disease.
Seo BA, Kim D, Hwang H, Kim MS, Ma SX, Kwon SH, Kweon SH, Wang H, Yoo JM, Choi S, Kwon SH, Kang SU, Kam TI, Kim K, Karuppagounder SS, Kang BG, Lee S, Park H, Kim S, Yan W, Li YS, Kuo SH, Redding-Ochoa J, Pletnikova O, Troncoso JC, Lee G, Mao X, Dawson VL, Dawson TM, Ko HS. Seo BA, et al. Neuron. 2021 Dec 1;109(23):3758-3774.e11. doi: 10.1016/j.neuron.2021.09.031. Epub 2021 Oct 12. Neuron. 2021. PMID: 34644545 Free PMC article.
In this paper, we identify the E3 ligase Thyroid Hormone Receptor Interacting Protein 12 (TRIP12) as a key regulator of GCase. TRIP12 interacts with and ubiquitinates GCase at lysine 293 to control its degradation via ubiquitin proteasomal degradation. ...TRIP12 …
In this paper, we identify the E3 ligase Thyroid Hormone Receptor Interacting Protein 12 (TRIP12) as a key regulator of GCase. TRI …
TRIP12's role in the governance of DNA polymerase beta involvement in DNA damage response and repair.
Inanc B, Fang Q, Roos WP, Andrews JF, Zeng X, Clark J, Li J, Dey NB, Ibrahim M, Sykora P, Yu Z, Pearson CR, Braganza A, Verheij M, Jonkers J, Yates NA, Vens C, Sobol RW. Inanc B, et al. Nucleic Acids Res. 2025 Jun 20;53(12):gkaf574. doi: 10.1093/nar/gkaf574. Nucleic Acids Res. 2025. PMID: 40613707 Free PMC article.
Required for Polbeta foci formation, TRIP12 influences Polbeta involvement after radiation-induced DNA damage, a process regulated by TRIP12-mediated ubiquitylation of Polbeta. ...The herein discovered function of TRIP12, in the governance of Polbeta-directed …
Required for Polbeta foci formation, TRIP12 influences Polbeta involvement after radiation-induced DNA damage, a process regulated by …
TRIP12 promotes small-molecule-induced degradation through K29/K48-branched ubiquitin chains.
Kaiho-Soma A, Akizuki Y, Igarashi K, Endo A, Shoda T, Kawase Y, Demizu Y, Naito M, Saeki Y, Tanaka K, Ohtake F. Kaiho-Soma A, et al. Mol Cell. 2021 Apr 1;81(7):1411-1424.e7. doi: 10.1016/j.molcel.2021.01.023. Epub 2021 Feb 9. Mol Cell. 2021. PMID: 33567268 Free article.
TRIP12 associates with BRD4 via CRL2(VHL) and specifically assembles K29-linked ubiquitin chains, facilitating the formation of K29/K48-branched ubiquitin chains and accelerating the assembly of K48 linkage by CRL2(VHL). Consequently, TRIP12 promotes the PROTAC-indu …
TRIP12 associates with BRD4 via CRL2(VHL) and specifically assembles K29-linked ubiquitin chains, facilitating the formation of K29/K …
Engineered targeting OIP5 sensitizes bladder cancer to chemotherapy resistance via TRIP12-PPP1CB-YBX1 axis.
Wang X, Guo T, Niu L, Zheng B, Huang W, Xu H, Huang W. Wang X, et al. Oncogene. 2024 Sep;43(38):2850-2867. doi: 10.1038/s41388-024-03136-8. Epub 2024 Aug 18. Oncogene. 2024. PMID: 39155295
In the present study, we show that gemcitabine plus cisplatin (GEM/DDP) therapy induces NF-kappaB signaling, which promotes p65-mediated transcriptional activation of OIP5. OIP5 recruits the E3 ubiquitin ligase TRIP12 to bind to and degrade the phosphatase PPP1CB, thereby …
In the present study, we show that gemcitabine plus cisplatin (GEM/DDP) therapy induces NF-kappaB signaling, which promotes p65-mediated tra …
TRIP12 governs DNA Polymerase beta involvement in DNA damage response and repair.
Inanc B, Fang Q, Andrews JF, Zeng X, Clark J, Li J, Dey NB, Ibrahim M, Sykora P, Yu Z, Braganza A, Verheij M, Jonkers J, Yates NA, Vens C, Sobol RW. Inanc B, et al. bioRxiv [Preprint]. 2024 Apr 10:2024.04.08.588474. doi: 10.1101/2024.04.08.588474. bioRxiv. 2024. Update in: Nucleic Acids Res. 2025 Jun 20;53(12):gkaf574. doi: 10.1093/nar/gkaf574. PMID: 38645048 Free PMC article. Updated. Preprint.
We find that DNA polymerase beta (Polbeta), crucial for BER, is ubiquitylated in a BER complex-dependent manner by TRIP12, an E3 ligase that partners with UBR5 and restrains DSB repair signaling. Here we find that, TRIP12, but not UBR5, controls cellular levels and …
We find that DNA polymerase beta (Polbeta), crucial for BER, is ubiquitylated in a BER complex-dependent manner by TRIP12, an E3 liga …
Dynamic regulation of the oxidative stress response by the E3 ligase TRIP12.
Ingersoll AJ, McCloud DM, Hu JY, Rape M. Ingersoll AJ, et al. bioRxiv [Preprint]. 2024 Nov 25:2024.11.25.625235. doi: 10.1101/2024.11.25.625235. bioRxiv. 2024. Update in: Cell Rep. 2025 Sep 23;44(9):116262. doi: 10.1016/j.celrep.2025.116262. PMID: 39651249 Free PMC article. Updated. Preprint.
TRIP12 is a ubiquitin chain elongation factor that cooperates with CUL3 (KEAP1) to ensure robust NRF2 degradation. In this manner, TRIP12 accelerates stress response silencing as ROS are being cleared, but limits NRF2 activation during stress. ...
TRIP12 is a ubiquitin chain elongation factor that cooperates with CUL3 (KEAP1) to ensure robust NRF2 degradation. In this manner, …
135 results