Evidence map›Paper›PMID 23453757›Full record

ArticleCell2013

Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins.

Nathan W Pierce, J Eugene Lee, Xing Liu, Michael J Sweredoski, Robert L J Graham, Elizabeth A Larimore, Michael Rome, Ning Zheng, Bruce E Clurman, Sonja Hess and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 163 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
163citing papers in PubMed, 1 pooled it
11.4field-weighted citation impact, top 1% 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

163 citing papers in PubMed, 1 synthesis or guideline pooled it, 258 citations in OpenAlex.

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  20. Structure and dynamics of a pentameric KCTD5/CUL3/Gβγ E3 ubiquitin ligase complex.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 4 institutions in 4 countries.

Nathan W PierceDivision of Biology, MC 156-29, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA.
J Eugene Lee
Xing Liu
Michael J Sweredoski
Robert L J Graham
Elizabeth A Larimore
Michael Rome
Ning Zheng
Bruce E Clurman
Sonja Hess
Shu-ou Shan
Raymond J Deshaies
California Institute of Technology · USFred Hutch Cancer Center · USHoward Hughes Medical Institute · USUniversity of Washington · US

Funding

Interdisciplinary Tranining in Cancer ResearchT32CA080416 · NCI · UNIVERSITY OF WASHINGTON · PI STODDARD, BARRY L. · 1998 to 2023
$9.7M
Tumor Suppression by the Fbw7 Ubiquitin LigaseR01CA084069 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI CLURMAN, BRUCE E · 2000 to 2015
$5.1M
Regulation of cullin - RING ubiquitin ligasesR01GM065997 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI DESHAIES, RAYMOND J · 2002 to 2018
$4.5M
Proteome-wide protein Identification Facilitated by in Vivo Cross-linkingF32CA138126 · NCI · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI LEE, JINHWAN EUGENE · 2009 to 2011
$162k
Howard Hughes Medical InstituteNCI NIH HHS CA138126NCI NIH HHS F32 CA138126NCI NIH HHS R01 CA084069NCI NIH HHS T32 CA080416NIGMS NIH HHS GM065997NIGMS NIH HHS R01 GM065997PHS HHS 10565784
6 · The paper itself

Abstract

The modular SCF (Skp1, cullin, and F box) ubiquitin ligases feature a large family of F box protein substrate receptors that enable recognition of diverse targets. However, how the repertoire of SCF complexes is sustained remains unclear. Real-time measurements of formation and disassembly indicate that SCF(Fbxw7) is extraordinarily stable, but, in the Nedd8-deconjugated state, the cullin-binding protein Cand1 augments its dissociation by one-million-fold. Binding and ubiquitylation assays show that Cand1 is a protein exchange factor that accelerates the rate at which Cul1-Rbx1 equilibrates with multiple F box protein-Skp1 modules. Depletion of Cand1 from cells impedes recruitment of new F box proteins to pre-existing Cul1 and profoundly alters the cellular landscape of SCF complexes. We suggest that catalyzed protein exchange may be a general feature of dynamic macromolecular machines and propose a hypothesis for how substrates, Nedd8, and Cand1 collaborate to regulate the cellular repertoire of SCF complexes.

Indexed as

AnimalsCell LineCullin ProteinsEscherichia coliF-Box ProteinsHumansMass SpectrometrySKP Cullin F-Box Protein LigasesTranscription FactorsCAND1 protein, humanCullin 1Cullin ProteinsF-Box ProteinsSKP Cullin F-Box Protein LigasesTranscription Factors

Identifiers

PMID23453757
PMCPMC3656483
OpenAlexW2149650548

What OpenQuestion holds

Textmetadata
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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 OpenQuestion graph.