Evidence map›Paper›PMID 28209614›Full record

ArticleCancer research2017

Distinct Interactions of EBP1 Isoforms with FBXW7 Elicits Different Functions in Cancer.

Yuli Wang, Pengju Zhang, Yunshan Wang, Panpan Zhan, Chunyan Liu, Jian-Hua Mao, Guangwei Wei

Open access · bronzeAbstract read
In one paragraph

Article in Cancer research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.

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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 2 institutions in 2 countries.

Yuli WangDepartment of Human Anatomy and Key Laboratory of Experimental Teratology, Ministry of Education, Shandong University School of Medicine, Shandong, PR China.
Pengju ZhangDepartment of Biochemistry and Molecular Biology, Shandong University School of Medicine, Shandong, PR China.
Yunshan WangDepartment of Human Anatomy and Key Laboratory of Experimental Teratology, Ministry of Education, Shandong University School of Medicine, Shandong, PR China.
Panpan ZhanDepartment of Biochemistry and Molecular Biology, Shandong University School of Medicine, Shandong, PR China.
Chunyan LiuDepartment of Biochemistry and Molecular Biology, Shandong University School of Medicine, Shandong, PR China.
Jian-Hua MaoBiological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, California. gwwei@yahoo.com JHMao@lbl.gov.
Guangwei WeiDepartment of Human Anatomy and Key Laboratory of Experimental Teratology, Ministry of Education, Shandong University School of Medicine, Shandong, PR China. gwwei@yahoo.com JHMao@lbl.gov.
Shandong University · CNLawrence Berkeley National Laboratory · US

Funding

The Role of Fbxw7 in genetic instability and cancerR01CA116481 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MAO, JIAN-HUA · 2008 to 2012
$1.7M
NCI NIH HHS R01 CA116481
6 · The paper itself

Abstract

The ErbB3 receptor-binding protein EBP1 encodes two alternatively spliced isoforms P48 and P42. While there is evidence of differential roles for these isoforms in tumorigenesis, little is known about their underlying mechanisms. Here, we demonstrate that EBP1 isoforms interact with the SCF-type ubiquitin ligase FBXW7 in distinct ways to exert opposing roles in tumorigenesis. EBP1 P48 bound to the WD domain of FBXW7 as an oncogenic substrate of FBXW7. EBP1 P48 binding sequestered FBXW7α to the cytosol, modulating its role in protein degradation and attenuating its tumor suppressor function. In contrast, EBP1 P42 bound to both the F-box domain of FBXW7 as well as FBXW7 substrates. This adapter function of EBP1 P42 stabilized the interaction of FBXW7 with its substrates and promoted FBXW7-mediated degradation of oncogenic targets, enhancing its overall tumor-suppressing function. Overall, our results establish distinct physical and functional interactions between FBXW7 and EBP1 isoforms, which yield their mechanistically unique isoform-specific functions of EBP1 in cancer.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsBinding SitesCell Cycle ProteinsCell Line, TumorCytoplasmF-Box ProteinsF-Box-WD Repeat-Containing Protein 7Glycogen Synthase Kinase 3 betaHCT116 CellsHEK293 CellsHeterograftsHumansImmunohistochemistryMiceMice, NudeAdaptor Proteins, Signal TransducingCell Cycle ProteinsF-Box ProteinsF-Box-WD Repeat-Containing Protein 7FBXW7 protein, humanGlycogen Synthase Kinase 3 betaPA2G4 protein, humanProteasome Endopeptidase ComplexProtein IsoformsRNA-Binding ProteinsUbiquitin-Protein Ligases

Identifiers

PMID28209614
PMCPMC5392370
OpenAlexW2588001676

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.