ArticleThe Journal of biological chemistry2015
EDD, a ubiquitin-protein ligase of the N-end rule pathway, associates with spindle assembly checkpoint components and regulates the mitotic response to nocodazole.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Cryo-EM structure of the chain-elongating E3 ubiquitin ligase UBR5.The EMBO journal · 2023Article
- UBR5 Acts as an Antiviral Host Factor against MERS-CoV via Promoting Ubiquitination and Degradation of ORF4b.Journal of virology · 2022Article
- The E3 ubiquitin ligase HECTD1 contributes to cell proliferation through an effect on mitosis.Scientific reports · 2022Article
- Role of ubiquitin-protein ligase UBR5 in the disassembly of mitotic checkpoint complexes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- UBR5 oncogene as an indicator of poor prognosis in gastric cancer.Experimental and therapeutic medicine · 2020Article
- Aurora B opposes PP1 function in mitosis by phosphorylating the conserved PP1-binding RVxF motif in PP1 regulatory proteins.Science signaling · 2018Article
- Assembly and Function of Heterotypic Ubiquitin Chains in Cell-Cycle and Protein Quality Control.Cell · 2017Article
- Normal human cell proteins that interact with the adenovirus type 5 E1B 55kDa protein.Virology · 2017Article
- BMI1-UBR5 axis regulates transcriptional repression at damaged chromatin.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- UBR-5, a Conserved HECT-Type E3 Ubiquitin Ligase, Negatively Regulates Notch-Type Signaling in Caenorhabditis elegans.G3 (Bethesda, Md.) · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In this work, we identify physical and genetic interactions that implicate E3 identified by differential display (EDD) in promoting spindle assembly checkpoint (SAC) function. During mitosis, the SAC initiates a mitotic checkpoint in response to chromosomes with kinetochores unattached to spindle pole microtubules. Similar to Budding uninhibited by benzimidazoles-related 1 (BUBR1) siRNA, a bona fide SAC component, EDD siRNA abrogated G2/M accumulation in response to the mitotic destabilizing agent nocodazole. Furthermore, EDD siRNA reduced mitotic cell viability and, in nocodazole-treated cells, increased expression of the promitotic progression protein cell division cycle 20 (CDC20). Copurification studies also identified physical interactions with CDC20, BUBR1, and other components of the SAC. Taken together, these observations highlight the potential role of EDD in regulating mitotic progression and the cellular response to perturbed mitosis.
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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.