Evidence map›Paper›PMID 33264605›Full record

ArticleStructure (London, England : 1993)2021

Cryo-EM structure of CtBP2 confirms tetrameric architecture.

Anne M Jecrois, M Michael Dcona, Xiaoyan Deng, Dipankar Bandyopadhyay, Steven R Grossman, Celia A Schiffer, William E Royer

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 21% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.

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  20. Tête-à-tête with CtBP dimers.Structure (London, England : 1993) · 2021
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Anne M JecroisDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
M Michael DconaDepartment of Internal Medicine, Virginia Commonwealth University, Richmond, VA 23298, USA.
Xiaoyan DengDepartment of Biostatistics, Virginia Commonwealth University, Richmond, VA 23298, USA.
Dipankar BandyopadhyayDepartment of Biostatistics, Virginia Commonwealth University, Richmond, VA 23298, USA; Massey Cancer Center, Virginia Commonwealth University, Richmond, VA 23298, USA.
Steven R GrossmanDepartment of Internal Medicine, Virginia Commonwealth University, Richmond, VA 23298, USA; Massey Cancer Center, Virginia Commonwealth University, Richmond, VA 23298, USA.
Celia A SchifferDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
William E RoyerDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA. Electronic address: william.royer@umassmed.edu.
Virginia Commonwealth University · USUniversity of Massachusetts Chan Medical School · US

Funding

Virus Vector Shared ResourceP30CA016059 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI Kim Felder Rhoads · 1985 to 2026
$51.0M
Structure-based characterization of CtBP as a therapeutic target in cancerR01GM119014 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI ROYER, WILLIAM E · 2017 to 2020
$1.3M
Structural Regulation of IRF3 Activation and Association with Co-activators of the IFN Beta EnhanceosomeF31GM129988 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI JECROIS, ANNE · 2018 to 2021
$91k
NCI NIH HHS P30 CA016059NIGMS NIH HHS F31 GM129988NIGMS NIH HHS R01 GM119014
6 · The paper itself

Abstract

C-terminal binding proteins 1 and 2 (CtBP1 and CtBP2) are transcriptional regulators that activate or repress many genes involved in cellular development, apoptosis, and metastasis. NADH-dependent CtBP activation has been implicated in multiple types of cancer and poor patient prognosis. Central to understanding activation of CtBP in oncogenesis is uncovering how NADH triggers protein assembly, what level of assembly occurs, and if oncogenic activity depends upon such assembly. Here, we present the cryoelectron microscopic structures of two different constructs of CtBP2 corroborating that the native state of CtBP2 in the presence of NADH is tetrameric. The physiological relevance of the observed tetramer was demonstrated in cell culture, showing that CtBP tetramer-destabilizing mutants are defective for cell migration, transcriptional repression of E-cadherin, and activation of TIAM1. Together with our cryoelectron microscopy studies, these results highlight the tetramer as the functional oligomeric form of CtBP2.

Indexed as

Protein MultimerizationAlcohol OxidoreductasesCadherinsCatalytic DomainCell MovementCo-Repressor ProteinsCryoelectron MicroscopyDNA-Binding ProteinsGene Expression Regulation, NeoplasticHCT116 CellsHumansMutationNADPProtein BindingT-Lymphoma Invasion and Metastasis-inducing Protein 1Alcohol OxidoreductasesCadherinsCo-Repressor ProteinsCTBP2 protein, humanC-terminal binding proteinDNA-Binding ProteinsNADPTIAM1 protein, humanT-Lymphoma Invasion and Metastasis-inducing Protein 1cancerC-terminal binding-protein CtBPmetastasistetrameric assemblyTIAM1transcription regulation

Identifiers

PMID33264605
PMCPMC9159756
OpenAlexW3016352913

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.