Evidence map›Paper›PMID 30482618›Full record

ReviewTrends in cell biology2019

Posing the APC/C E3 Ubiquitin Ligase to Orchestrate Cell Division.

Edmond R Watson, Nicholas G Brown, Jan-Michael Peters, Holger Stark, Brenda A Schulman

Open access · greenAbstract readReview
In one paragraph

Review in Trends in cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
7.6field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

83 citing papers in PubMed, 153 citations in OpenAlex.

  1. Article
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  17. Review
  18. Cryo-EM structures of apo-APC/C and APC/CNature communications · 2024
    Article
  19. Article
  20. Article

23 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 4 institutions in 3 countries.

Edmond R WatsonDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, 82152, Germany.
Nicholas G BrownDepartment of Pharmacology and Lineberger Comprehensive Cancer Center, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
Jan-Michael PetersResearch Institute of Molecular Pathology (IMP), Campus Vienna Biocenter (VBC) 1, 1030 Vienna, Austria.
Holger StarkMax Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Brenda A SchulmanDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, 82152, Germany; Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA. Electronic address: schulman@biochem.mpg.de.
Max Planck Institute of Biochemistry · DEMax Planck Institute for Biophysical Chemistry · DEResearch Institute of Molecular Pathology · ATUNC Lineberger Comprehensive Cancer Center

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI Shondra Michelle Miller · 1985 to 2026
$166.9M
Spindle Assembly Checkpoint SilencingR35GM128855 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Nicholas Gene Brown · 2018 to 2026
$4.1M
E3-mediated Ubiquitin-like Protein LigationR37GM069530 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHULMAN, BRENDA A · 2014 to 2018
$2.0M
NCI NIH HHS P30 CA021765NIGMS NIH HHS R35 GM128855NIGMS NIH HHS R37 GM069530
6 · The paper itself

Abstract

The anaphase promoting complex/cyclosome (APC/C) E3 ligase controls mitosis and nonmitotic pathways through interactions with proteins that coordinate ubiquitylation. Since the discovery that the catalytic subunits of APC/C are conformationally dynamic cullin and RING proteins, many unexpected and intricate regulatory mechanisms have emerged. Here, we review structural knowledge of this regulation, focusing on: (i) coactivators, E2 ubiquitin (Ub)-conjugating enzymes, and inhibitors engage or influence multiple sites on APC/C including the cullin-RING catalytic core; and (ii) the outcomes of these interactions rely on mobility of coactivators and cullin-RING domains, which permits distinct conformations specifying different functions. Thus, APC/C is not simply an interaction hub, but is instead a dynamic, multifunctional molecular machine whose structure is remodeled by binding partners to achieve temporal ubiquitylation regulating cell division.

Indexed as

MitosisAnaphase-Promoting Complex-CyclosomeCarrier ProteinsHumansModels, MolecularProtein BindingProtein ConformationUbiquitinationUbiquitin-Protein LigasesAnaphase-Promoting Complex-CyclosomeCarrier ProteinsUbiquitin-Protein Ligasesanaphase promoting complex/cyclosomecell divisioncryo-electron microscopyE3 ligasemitosisubiquitin

Identifiers

PMID30482618
PMCPMC6340778
OpenAlexW2898104208

What Socratic holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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 Socratic graph.