| ARIH2 regulates the proliferation, DNA damage and chemosensitivity of gastric cancer cells by reducing the stability of p21 via ubiquitination. | ARIH2 regulates the proliferation, DNA damage and chemosensitivity of gastric cancer cells by reducing the stability of p21 via ubiquitination.
Geng S, Peng W, Wang X, Hu X, Liang H, Hou J, Wang F, Zhao G, Lü M, Cui H., Free PMC Article | 07/2/2022 |
| Here, using a quantitative proteomics approach, the authors identify the E3 ligase ARIH2 as a regulator of the HIV-1 Vif protein-dependent CRL5-mediated APOBEC3 degradation. The CUL5(Vif/CBFss) complex recruits ARIH2 where it acts to transfer ubiquitin directly to the APOBEC3 targets. | ARIH2 Is a Vif-Dependent Regulator of CUL5-Mediated APOBEC3G Degradation in HIV Infection.
Hüttenhain R, Xu J, Burton LA, Gordon DE, Hultquist JF, Johnson JR, Satkamp L, Hiatt J, Rhee DY, Baek K, Crosby DC, Frankel AD, Marson A, Harper JW, Alpi AF, Schulman BA, Gross JD, Krogan NJ., Free PMC Article | 11/23/2019 |
| ubiquitin-associated (UBA) domain-containing DCNL1 is monoubiquitylated when bound to CRLs and that this monoubiquitylation depends on the CRL-associated Ariadne RBR ligases TRIAD1 (ARIH2) and HHARI (ARIH1) and strictly requires the DCNL1's UBA domain. | Coupled monoubiquitylation of the co-E3 ligase DCNL1 by Ariadne-RBR E3 ubiquitin ligases promotes cullin-RING ligase complex remodeling.
Kelsall IR, Kristariyanto YA, Knebel A, Wood NT, Kulathu Y, Alpi AF., Free PMC Article | 05/4/2019 |
| Data found Mll-Ell increases Triad1 in a Hox-dependent manner. Triad1 antagonizes Mll-Ell-induced protein ubiquitination and progression to AML. Triad1 knockdown significantly shortened the latency to development of AML in mice transplanted with Mll-Ell-transduced bone marrow. Further results identify Triad1 as a leukemia suppressor in 11q23-AML. | The E3 ubiquitin ligase Triad1 influences development of Mll-Ell-induced acute myeloid leukemia.
Wang H, Bei L, Shah CA, Huang W, Platanias LC, Eklund EA., Free PMC Article | 02/23/2019 |
| these findings reveal a novel mechanism of ubiquitination-dependent negative regulation of the NLRP3 inflammasome by ARIH2 and highlight ARIH2 as a potential therapeutic target for inflammatory diseases | ARIH2 Ubiquitinates NLRP3 and Negatively Regulates NLRP3 Inflammasome Activation in Macrophages.
Kawashima A, Karasawa T, Tago K, Kimura H, Kamata R, Usui-Kawanishi F, Watanabe S, Ohta S, Funakoshi-Tago M, Yanagisawa K, Kasahara T, Suzuki K, Takahashi M. | 11/25/2017 |
| We show that ARIH2 E3-ligase regulates PABPN1 protein accumulation and aggregation | A novel feed-forward loop between ARIH2 E3-ligase and PABPN1 regulates aging-associated muscle degeneration.
Raz V, Buijze H, Raz Y, Verwey N, Anvar SY, Aartsma-Rus A, van der Maarel SM. | 12/6/2014 |
| TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes. | TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes.
Kelsall IR, Duda DM, Olszewski JL, Hofmann K, Knebel A, Langevin F, Wood N, Wightman M, Schulman BA, Alpi AF., Free PMC Article | 01/4/2014 |
| study demonstrated that TRIAD1 is a ubiquitination target for proteasome-dependent degradation by MDM2; results suggest TRIAD1 degradation by MDM2 suppresses TRIAD1-mediated cell growth; data suggested a novel negative regulatory mechanism of TRIAD1 via MDM2 E3 ligase ubiquitination | TRIAD1 is negatively regulated by the MDM2 E3 ligase.
Bae S, Jung JH, An IS, Kim OY, Lee MJ, Lee JH, Park IC, Lee SJ, An S. | 03/16/2013 |
| TRIAD1 as a novel modulator of the p53-MDM2 axis that induces p53 activation by inhibiting its regulation by MDM2. | TRIAD1 inhibits MDM2-mediated p53 ubiquitination and degradation.
Bae S, Jung JH, Kim K, An IS, Kim SY, Lee JH, Park IC, Jin YW, Lee SJ, An S. | 12/8/2012 |
| In sharp contrast to SIAH1/SIAH2 and UBCH8, TRIAD1 binding to PML-RARalpha has no effect on its turnover. | Differential regulation of PML-RARα stability by the ubiquitin ligases SIAH1/SIAH2 and TRIAD1.
Pietschmann K, Buchwald M, Müller S, Knauer SK, Kögl M, Heinzel T, Krämer OH. | 07/14/2012 |
| HoxA10 influences protein ubiquitination by activating transcription of ARIH2, the gene encoding Triad1 | HoxA10 influences protein ubiquitination by activating transcription of ARIH2, the gene encoding Triad1.
Wang H, Bei L, Shah CA, Horvath E, Eklund EA., Free PMC Article | 07/16/2011 |
| Triad1 has dual ubiquitin ligase activity; both its RING domains are crucial for inhibiting myeloid proliferation. The N-terminal RING finger (RING1) of Triad1 binds UbcH7; the C-terminal RING finger (RING2) binds Ubc13. | The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains.
Marteijn JA, van der Meer LT, Smit JJ, Noordermeer SM, Wissink W, Jansen P, Swarts HG, Hibbert RG, de Witte T, Sixma TK, Jansen JH, van der Reijden BA. | 01/21/2010 |
| The fine-tuning of Gfi1 protein levels regulated by Triad1 defines an unexpected role for this protein in hematopoiesis. | Gfi1 ubiquitination and proteasomal degradation is inhibited by the ubiquitin ligase Triad1.
Marteijn JA, van der Meer LT, van Emst L, van Reijmersdal S, Wissink W, de Witte T, Jansen JH, Van der Reijden BA. | 01/21/2010 |
| proteasomal degradation of proteins that are ubiquitinated by Triad1 affects the clonogenic growth of primary myeloid progenitor cells | The E3 ubiquitin-protein ligase Triad1 inhibits clonogenic growth of primary myeloid progenitor cells.
Marteijn JA, van Emst L, Erpelinck-Verschueren CA, Nikoloski G, Menke A, de Witte T, Löwenberg B, Jansen JH, van der Reijden BA. | 01/21/2010 |