ArticleThe Journal of biological chemistry2011
Transcription factor IIS cooperates with the E3 ligase UBR5 to ubiquitinate the CDK9 subunit of the positive transcription elongation factor B.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 42 citations in OpenAlex.
- Nuclear ubiquitination permits Hippo-YAP signal for liver development and tumorigenesis.Nature chemical biology · 2025Article
- Deriving general structure-activity/selectivity relationship patterns for different subfamilies of cyclin-dependent kinase inhibitors using machine learning methods.Scientific reports · 2024Article
- DNMT1-mediated epigenetic suppression of FBXO32 expression promoting cyclin dependent kinase 9 (CDK9) survival and esophageal cancer cell growth.Cell cycle (Georgetown, Tex.) · 2024Article
- Structure of the human UBR5 E3 ubiquitin ligase.Structure (London, England : 1993) · 2023Article
- CSN6 promotes melanoma proliferation and metastasis by controlling the UBR5-mediated ubiquitination and degradation of CDK9.Cell death & disease · 2021Article
- UBR5 oncogene as an indicator of poor prognosis in gastric cancer.Experimental and therapeutic medicine · 2020Article
- UBR5 HECT domain mutations identified in mantle cell lymphoma control maturation of B cells.Blood · 2020Article
- E3 ubiquitin ligases in B-cell malignancies.Cellular immunology · 2019Review
- TCEA1 regulates the proliferative potential of mouse myeloid cells.Experimental cell research · 2018Article
- UBR5 Contributes to Colorectal Cancer Progression by Destabilizing the Tumor Suppressor ECRG4.Digestive diseases and sciences · 2017Article
- Downregulation of the proapoptotic protein MOAP-1 by the UBR5 ubiquitin ligase and its role in ovarian cancer resistance to cisplatin.Oncogene · 2017Article
- BMI1-UBR5 axis regulates transcriptional repression at damaged chromatin.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- ELL targets c-Myc for proteasomal degradation and suppresses tumour growth.Nature communications · 2016Article
- Role of Ostm1 Cytosolic Complex with Kinesin 5B in Intracellular Dispersion and Trafficking.Molecular and cellular biology · 2016Article
- The MLLE domain of the ubiquitin ligase UBR5 binds to its catalytic domain to regulate substrate binding.The Journal of biological chemistry · 2015Article
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- Hyperplastic discs differentially regulates the transcriptional outputs of hedgehog signaling.Mechanisms of development · 2014Article
- Microarray characterization of gene expression changes in blood during acute ethanol exposure.BMC medical genomics · 2013Article
- Proteomics-based methods for discovery, quantification, and validation of protein-protein interactions.Analytical chemistry · 2013Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Elongation of transcription by mammalian RNA polymerase II (RNAPII) is regulated by specific factors, including transcription factor IIS (TFIIS) and positive transcription elongation factor b (P-TEFb). We show that the E3 ubiquitin ligase UBR5 associates with the CDK9 subunit of positive transcription elongation factor b to mediate its polyubiquitination in human cells. TFIIS also binds UBR5 to stimulate CDK9 polyubiquitination. Co-localization of UBR5, CDK9, and TFIIS along specific regions of the γ fibrinogen (γFBG) gene indicates that a ternary complex involving these factors participates in the transcriptional regulation of this gene. In support of this notion, overexpression of TFIIS not only modifies the ubiquitination pattern of CDK9 in vivo but also increases the association of CDK9 with various regions of the γFBG gene. Notably, the TFIIS-mediated increase in CDK9 loading is obtained during both basal and activated transcription of the γFBG gene. This increased CDK9 binding is paralleled by an increase in the recruitment of RNAPII along the γFBG gene and the phosphorylation of the C-terminal domain of the RNAPII largest subunit RPB1 on Ser-2, a known target of CDK9. Together, these results identify UBR5 as a novel E3 ligase that regulates transcription and define an additional function of TFIIS in the regulation of CDK9.
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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.