Evidence map›Paper›PMID 23658844›Full record

ArticlePloS one2013

The novel ubiquitin ligase complex, SCF(Fbxw4), interacts with the COP9 signalosome in an F-box dependent manner, is mutated, lost and under-expressed in human cancers.

William W Lockwood, Sahiba K Chandel, Greg L Stewart, Hediye Erdjument-Bromage, Levi J Beverly

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

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  9. Beneficial effects of an endogenous enrichment in n3-PUFAs on Wnt signaling are associated with attenuation of alcohol-mediated liver disease in mice.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  10. Article
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  12. Review
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  14. Ubiquitination-mediated degradation of cell cycle-related proteins by F-box proteins.The international journal of biochemistry & cell biology · 2016
    Review
  15. Review
  16. Roles of F-box proteins in cancer.Nature reviews. Cancer · 2014
    Review
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 2 countries.

William W LockwoodCancer Biology and Genetics Section, Cancer Genetics Branch, National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland, United States of America.
Sahiba K Chandel
Greg L Stewart
Hediye Erdjument-Bromage
Levi J Beverly
University of Louisville · USBC Cancer Agency · CAMemorial Sloan Kettering Cancer Center · USNational Human Genome Research Institute · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
The Role of Id Proteins in Breast TumorigenesisP01CA094060 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI NORTON, LARRY · 2002 to 2018
$39.4M
The Role of Focal Oncogene Amplifications in Lung CancerP01CA129243 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI Piro Lito · 2007 to 2026
$31.2M
Molecular Targets COBREP20GM103482 · NIGMS · UNIVERSITY OF LOUISVILLE · PI MILLER, DONALD M. · 2012 to 2012
$2.0M
Intramural NIH HHSNCI NIH HHS P01 CA094060NCI NIH HHS P01 CA129243NCI NIH HHS P01 CA129243-01NCI NIH HHS P01 CA94060NCI NIH HHS P30 CA008748NCI NIH HHS P30 CA08748NIGMS NIH HHS 8P20GM103482-10NIGMS NIH HHS P20 GM103482
6 · The paper itself

Abstract

Identification of novel proteins that can potentially contribute to carcinogenesis is a requisite venture. Herein, we report the first biochemical characterization of the novel F-box and WD40 containing protein, FBXW4. We have identified interacting protein partners and demonstrated that FBXW4 is part of a ubiquitin ligase complex. Furthermore, the Fbxw4 locus is a common site of proviral insertion in a variety of retroviral insertional mutagenesis murine cancer models and Fbxw4 mRNA is highly expressed in the involuting murine mammary gland. To begin to characterize the biochemical function of Fbxw4, we used proteomic analysis to demonstrate that Fbxw4 interacts with Skp1 (SKP1), Cullin1 (CUL1), Ring-box1 (RBX1) and all components of the COP9 signalosome. All of these interactions are dependent on an intact F-box domain of Fbxw4. Furthermore, Fbxw4 is capable of interacting with ubiquitinated proteins within cells in an F-box dependent manner. Finally, we demonstrate that FBXW4 is mutated, lost and under-expressed in a variety of human cancer cell lines and clinical patient samples. Importantly, expression of FBXW4 correlates with survival of patients with non-small cell lung cancer. Taken together, we suggest that FBXW4 may be a novel tumor suppressor that regulates important cellular processes.

Indexed as

Gene Expression Regulation, NeoplasticMutationAnimalsCarcinoma, Non-Small-Cell LungCell Line, TumorCOP9 Signalosome ComplexF-Box MotifsF-Box ProteinsHumansLung NeoplasmsMiceMultiprotein ComplexesNeoplasmsPeptide HydrolasesProtein BindingProtein Structure, TertiaryCOP9 Signalosome ComplexF-Box ProteinsFBXW4 protein, humanMultiprotein ComplexesPeptide HydrolasesSKP Cullin F-Box Protein Ligases

Identifiers

PMID23658844
PMCPMC3642104
OpenAlexW2079929902

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.