ArticleOpen biology2013
Ubiquitination site preferences in anaphase promoting complex/cyclosome (APC/C) substrates.
Article in Open biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
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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
30 citing papers in PubMed, 46 citations in OpenAlex.
- Article
- Ubiquitin-Dependent and Independent Proteasomal Degradation in Host-Pathogen Interactions.Molecules (Basel, Switzerland) · 2023Review
- Revisiting degron motifs in human AURKA required for its targeting by APC/CLife science alliance · 2023Article
- Polypeptide N-acetylgalactosamine transferase 3: a post-translational writer on human health.Journal of molecular medicine (Berlin, Germany) · 2022Review
- Counting Degrons: Lessons From Multivalent Substrates for Targeted Protein Degradation.Frontiers in physiology · 2022Review
- Intricate Regulatory Mechanisms of the Anaphase-Promoting Complex/Cyclosome and Its Role in Chromatin Regulation.Frontiers in cell and developmental biology · 2021Review
- A unique binding mode of Nek2A to the APC/C allows its ubiquitination during prometaphase.EMBO reports · 2020Article
- Excess TPX2 Interferes with Microtubule Disassembly and Nuclei Reformation at Mitotic Exit.Cells · 2020Article
- 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
- Constitutive regulation of mitochondrial morphology by Aurora A kinase depends on a predicted cryptic targeting sequence at the N-terminus.Open biology · 2018Article
- The functional diversity of Aurora kinases: a comprehensive review.Cell division · 2018Review
- Differential Selective Pressures Experienced by the Aurora Kinase Gene Family.International journal of molecular sciences · 2017Article
- Features of reactive cysteines discovered through computation: from kinase inhibition to enrichment around protein degrons.Scientific reports · 2017Article
- Visualizing the complex functions and mechanisms of the anaphase promoting complex/cyclosome (APC/C).Open biology · 2017Review
- Quantitative proteomic analysis of Parkin substrates in Drosophila neurons.Molecular neurodegeneration · 2017Article
- APC/CDevelopmental cell · 2017Article
- Building a Regulatory Network with Short Linear Sequence Motifs: Lessons from the Degrons of the Anaphase-Promoting Complex.Molecular cell · 2016Review
- Design Principles Involving Protein Disorder Facilitate Specific Substrate Selection and Degradation by the Ubiquitin-Proteasome System.The Journal of biological chemistry · 2016Review
- Feedback regulation between atypical E2Fs and APC/CCdh1 coordinates cell cycle progression.EMBO reports · 2016Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Ordered progression of mitosis requires precise control in abundance of mitotic regulators. The anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase plays a key role by directing ubiquitin-mediated destruction of targets in a temporally and spatially defined manner. Specificity in APC/C targeting is conferred through recognition of substrate D-box and KEN degrons, while the specificity of ubiquitination sites, as another possible regulated dimension, has not yet been explored. Here, we present the first analysis of ubiquitination sites in the APC/C substrate ubiquitome. We show that KEN is a preferred ubiquitin acceptor in APC/C substrates and that acceptor sites are enriched in predicted disordered regions and flanked by serine residues. Our experimental data confirm a role for the KEN lysine as an ubiquitin acceptor contributing to substrate destruction during mitotic progression. Using Aurora A and Nek2 kinases as examples, we show that phosphorylation on the flanking serine residue could directly regulate ubiquitination and subsequent degradation of substrates. We propose a novel layer of regulation in substrate ubiquitination, via phosphorylation adjacent to the KEN motif, in APC/C-mediated targeting.
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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.