ArticleNature structural & molecular biology2011
Substrate binding on the APC/C occurs between the coactivator Cdh1 and the processivity factor Doc1.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
70 citing papers in PubMed, 108 citations in OpenAlex.
- Article
- A comparative study of the cryo-EM structures ofeLife · 2024Article
- Role of spindle assembly checkpoint proteins in gametogenesis and embryogenesis.Frontiers in cell and developmental biology · 2024Review
- Time-resolved cryo-EM (TR-EM) analysis of substrate polyubiquitination by the RING E3 anaphase-promoting complex/cyclosome (APC/C).Nature structural & molecular biology · 2023Article
- Examining the mechanistic relationship of APC/CProtein science : a publication of the Protein Society · 2022Article
- Counting Degrons: Lessons From Multivalent Substrates for Targeted Protein Degradation.Frontiers in physiology · 2022Review
- In silico analysis and molecular identification of an anaphase-promoting complex homologue from human pathogen Entamoeba histolytica.Journal, genetic engineering & biotechnology · 2021Article
- Using Budding Yeast to Identify Molecules That Block Cancer Cell 'Mitotic Slippage' Only in the Presence of Mitotic Poisons.International journal of molecular sciences · 2021Review
- Intricate Regulatory Mechanisms of the Anaphase-Promoting Complex/Cyclosome and Its Role in Chromatin Regulation.Frontiers in cell and developmental biology · 2021Review
- Review
- Ubiquitin chain-elongating enzyme UBE2S activates the RING E3 ligase APC/C for substrate priming.Nature structural & molecular biology · 2020Article
- Polyanions provide selective control of APC/C interactions with the activator subunit.Nature communications · 2019Article
- The pseudosubstrate inhibitor Acm1 inhibits the anaphase-promoting complex/cyclosome by combining high-affinity activator binding with disruption of Doc1/Apc10 function.The Journal of biological chemistry · 2019Article
- Anaphase-promoting complex/cyclosome regulates RdDM activity by degrading DMS3 inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Posing the APC/C E3 Ubiquitin Ligase to Orchestrate Cell Division.Trends in cell biology · 2019Review
- Mechanisms for the temporal regulation of substrate ubiquitination by the anaphase-promoting complex/cyclosome.Cell division · 2019Review
- APC/C: current understanding and future perspectives.F1000Research · 2019Review
- SUMO targets the APC/C to regulate transition from metaphase to anaphase.Nature communications · 2018Article
- Visualizing the complex functions and mechanisms of the anaphase promoting complex/cyclosome (APC/C).Open biology · 2017Review
- Review
10 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
The anaphase-promoting complex/cyclosome (APC/C) is a 22S ubiquitin ligase complex that initiates chromosome segregation and mitotic exit. We have used biochemical and electron microscopic analyses of Saccharomyces cerevisiae and human APC/C to address how the APC/C subunit Doc1 contributes to recruitment and processive ubiquitylation of APC/C substrates, and to understand how APC/C monomers interact to form a 36S dimeric form. We show that Doc1 interacts with Cdc27, Cdc16 and Apc1 and is located in the vicinity of the cullin-RING module Apc2-Apc11 in the inner cavity of the APC/C. Substrate proteins also bind in the inner cavity, in close proximity to Doc1 and the coactivator Cdh1, and induce conformational changes in Apc2-Apc11. Our results suggest that substrates are recruited to the APC/C by binding to a bipartite substrate receptor composed of a coactivator protein and Doc1.
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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.