Evidence map›Paper›PMID 29103612›Full record

ArticleCell2017

Composition and Regulation of the Cellular Repertoire of SCF Ubiquitin Ligases.

Justin M Reitsma, Xing Liu, Kurt M Reichermeier, Annie Moradian, Michael J Sweredoski, Sonja Hess, Raymond J Deshaies

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

91 citing papers in PubMed, 148 citations in OpenAlex.

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31 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

7 authors at 1 institution in 1 country.

Justin M ReitsmaDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
Xing LiuDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
Kurt M ReichermeierDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
Annie MoradianProteome Exploration Laboratory, Division of Biology and Biological Engineering, Beckman Institute, California Institute of Technology, Pasadena, CA 91125, USA.
Michael J SweredoskiProteome Exploration Laboratory, Division of Biology and Biological Engineering, Beckman Institute, California Institute of Technology, Pasadena, CA 91125, USA.
Sonja HessProteome Exploration Laboratory, Division of Biology and Biological Engineering, Beckman Institute, California Institute of Technology, Pasadena, CA 91125, USA.
Raymond J DeshaiesDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA; Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA. Electronic address: deshaies@caltech.edu.
California Institute of Technology · US

Funding

Regulation of cullin - RING ubiquitin ligasesR01GM065997 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI DESHAIES, RAYMOND J · 2002 to 2018
$4.5M
Mapping the dynamic assembly of SCF E3 ubiquitin ligases during the cell cycleF32GM112308 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI REITSMA, JUSTIN · 2014 to 2016
$157k
NIGMS NIH HHS F32 GM112308NIGMS NIH HHS R01 GM065997
6 · The paper itself

Abstract

SCF (Skp1-Cullin-F-box) ubiquitin ligases comprise several dozen modular enzymes that have diverse roles in biological regulation. SCF enzymes share a common catalytic core containing Cul1⋅Rbx1, which is directed toward different substrates by a variable substrate receptor (SR) module comprising 1 of 69 F-box proteins bound to Skp1. Despite the broad cellular impact of SCF enzymes, important questions remain about the architecture and regulation of the SCF repertoire, including whether SRs compete for Cul1 and, if so, how this competition is managed. Here, we devise methods that preserve the in vivo assemblages of SCF complexes and apply quantitative mass spectrometry to perform a census of these complexes (the "SCFome") in various states. We show that Nedd8 conjugation and the SR exchange factor Cand1 have a profound effect on shaping the SCFome. Together, these factors enable rapid remodeling of SCF complexes to promote biased assembly of SR modules bound to substrate.

Indexed as

Carrier ProteinsCell LineChromatography, AffinityCullin ProteinsHumansMass SpectrometryNEDD8 ProteinSKP Cullin F-Box Protein LigasesCarrier ProteinsCullin 1Cullin ProteinsNEDD8 ProteinNEDD8 protein, humanRBX1 protein, humanSKP Cullin F-Box Protein LigasesCop9 signalosomeCRLcullin-RINGE3 ligaseMRMproteasomeSRMubiquitin

Identifiers

PMID29103612
PMCPMC5711595
OpenAlexW2766427223

What OpenQuestion 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 OpenQuestion graph.