Evidence map›Paper›PMID 26097998›Full record

ArticleLaboratory investigation; a journal of technical methods and pathology2015

FBXW7 negatively regulates ENO1 expression and function in colorectal cancer.

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

Open access · bronzeAbstract read
In one paragraph

Article in Laboratory investigation; a journal of technical methods and pathology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed, 2 pooled it
2.9field-weighted citation impact, top 9% 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

47 citing papers in PubMed, 2 syntheses or guidelines pooled it, 78 citations in OpenAlex.

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  20. ENO1 and Cancer.Molecular therapy oncolytics · 2022
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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

9 authors at 2 institutions in 2 countries.

Panpan ZhanDepartment of Biochemistry and Molecular Biology, Shandong University School of Medicine, Shandong, P.R. China.
Yuli WangDepartment of Anatomy and Key Laboratory of Experimental Teratology, Ministry of Education, Shandong University School of Medicine, Shandong, P.R. China.
Shihu ZhaoDepartment of Biochemistry and Molecular Biology, Shandong University School of Medicine, Shandong, P.R. China.
Chunyan LiuDepartment of Biochemistry and Molecular Biology, Shandong University School of Medicine, Shandong, P.R. China.
Yunshan WangDepartment of Anatomy and Key Laboratory of Experimental Teratology, Ministry of Education, Shandong University School of Medicine, Shandong, P.R. China.
Mingxin WenDepartment of Anatomy and Key Laboratory of Experimental Teratology, Ministry of Education, Shandong University School of Medicine, Shandong, P.R. China.
Jian-Hua MaoLife Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
Guangwei WeiDepartment of Anatomy and Key Laboratory of Experimental Teratology, Ministry of Education, Shandong University School of Medicine, Shandong, P.R. China.
Pengju ZhangDepartment of Biochemistry and Molecular Biology, Shandong University School of Medicine, Shandong, P.R. China.
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

FBXW7 (F-box and WD40 domain protein 7) is a tumor suppressor frequently inactivated in human cancers. The precise molecular mechanisms by which FBXW7 exerts antitumor activity remain under intensive investigation and are thought to relate in part to FBXW7-mediated destruction of key cancer-relevant proteins. Enolase 1 (ENO1) possesses oncogenic activity and is often overexpressed in various human cancers, besides its critical role in glycolysis. However, the detailed regulatory mechanisms of ENO1 expression remain unclear. Here we show that the elevated expression of ENO1 was identified in FBXW7-depletion HCT116 cells through two-dimensional protein electrophoresis and mass spectrometry assays (2DE-MS). Subsequent western blotting and immunohistochemical assays confirmed that ENO1 expression reversely correlates with FBXW7 expression in several cells and colon cancer tissues. Furthermore, we show that FBXW7 physically binds to ENO1 and targets ENO1 for ubiquitin-mediated degradation. Functionally, we found that FBXW7 suppresses the ENO1-induced gene expression, lactate production, cell proliferation and migration. These findings suggest that ENO1 is a novel substrate of FBXW7, and its activity can be negatively regulated by FBXW7 at the posttranslational level. Our work provides a novel molecular insight into FBXW7-directed tumor suppression through regulation of ENO1.

Indexed as

Biomarkers, TumorBlotting, WesternCell Cycle ProteinsColorectal NeoplasmsDNA-Binding ProteinsDNA PrimersElectrophoresis, Gel, Two-DimensionalF-Box ProteinsF-Box-WD Repeat-Containing Protein 7Gene Expression Regulation, NeoplasticHCT116 CellsHumansImmunohistochemistryMass SpectrometryPhosphopyruvate HydrataseReal-Time Polymerase Chain ReactionBiomarkers, TumorCell Cycle ProteinsDNA-Binding ProteinsDNA PrimersENO1 protein, humanF-Box ProteinsF-Box-WD Repeat-Containing Protein 7FBXW7 protein, humanPhosphopyruvate HydrataseTumor Suppressor ProteinsUbiquitin-Protein Ligases

Identifiers

PMID26097998
PMCPMC4552619
OpenAlexW1749961819

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.