ArticleLeukemia2009
The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains.
Article in Leukemia, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 31 citations in OpenAlex.
- Review
- The roles of ubiquitination in AML.Annals of hematology · 2024Review
- ARIH2 regulates the proliferation, DNA damage and chemosensitivity of gastric cancer cells by reducing the stability of p21 via ubiquitination.Cell death & disease · 2022Article
- Triad1 Promotes the Inflammatory Response and Neuronal Apoptosis to Aggravate Acute Spinal Cord Injury in Rats.Computational and mathematical methods in medicine · 2022Article
- Mechanism and Disease Association With a Ubiquitin Conjugating E2 Enzyme: UBE2L3.Frontiers in immunology · 2022Review
- E3 ubiquitin ligase Wwp1 regulates ciliary dynamics of the Hedgehog receptor Smoothened.The Journal of cell biology · 2021Article
- The expression of TRIAD1 and DISC1 after traumatic brain injury and its influence on NSCs.Stem cell research & therapy · 2018Article
- E6AP/UBE3A catalyzes encephalomyocarditis virus 3C protease polyubiquitylation and promotes its concentration reduction in virus-infected cells.Biochemical and biophysical research communications · 2017Article
- Ubiquitin-Dependent Modification of Skeletal Muscle by the Parasitic Nematode, Trichinella spiralis.PLoS pathogens · 2016Article
- Ubc13: the Lys63 ubiquitin chain building machine.Oncotarget · 2016Review
- HoxA10 Terminates Emergency Granulopoiesis by Increasing Expression of Triad1.Journal of immunology (Baltimore, Md. : 1950) · 2015Article
- Targeting novel signaling pathways for resistant acute myeloid leukemia.Molecular genetics and metabolism · 2015Review
- RBR E3 ubiquitin ligases: new structures, new insights, new questions.The Biochemical journal · 2014Review
- RBR E3-ligases at work.EMBO reports · 2014Review
- Target specificity of the E3 ligase LUBAC for ubiquitin and NEMO relies on different minimal requirements.The Journal of biological chemistry · 2013Article
- ARIH2 is essential for embryogenesis, and its hematopoietic deficiency causes lethal activation of the immune system.Nature immunology · 2013Article
- The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension.The EMBO journal · 2012Article
- Identification of the ubiquitin ligase Triad1 as a regulator of endosomal transport.Biology open · 2012Article
- Genetic screen for regulators of lymph gland homeostasis and hemocyte maturation in Drosophila.G3 (Bethesda, Md.) · 2012Article
- HoxA10 influences protein ubiquitination by activating transcription of ARIH2, the gene encoding Triad1.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubiquitination plays a major role in many aspects of hematopoiesis. Alterations in ubiquitination have been implicated in hematological cancer. The ubiquitin ligase Triad1 controls the proliferation of myeloid cells. Here, we show that two RING (really interesting new gene) domains in Triad1 differentially bind ubiquitin-conjugating enzymes, UbcH7 and Ubc13. UbcH7 and Ubc13 are known to catalyze the formation of different poly-ubiquitin chains. These chains mark proteins for proteasomal degradation or serve crucial non-proteolytic functions, respectively. In line with the dual Ubc interactions, we observed that Triad1 catalyzes the formation of both types of ubiquitin chains. The biological relevance of this finding was studied by testing Triad1 mutants in myeloid clonogenic assays. Full-length Triad1 and three mutants lacking conserved domains inhibited myeloid colony formation by over 50%. Strikingly, deletion of either RING finger completely abrogated the inhibitory effect of Triad1 in clonogenic growth. We conclude that Triad1 exhibits dual ubiquitin ligase activity and that both of its RING domains are crucial to inhibit myeloid cell proliferation. The differential interaction of the RINGs with Ubcs strongly suggests that the ubiquitination mediated through UbcH7 as well as Ubc13 plays a major role in myelopoiesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.