Evidence map›Paper›PMID 24954416›Full record

ArticleCell metabolism2014

SDHAF4 promotes mitochondrial succinate dehydrogenase activity and prevents neurodegeneration.

Jonathan G Van Vranken, Daniel K Bricker, Noah Dephoure, Steven P Gygi, James E Cox, Carl S Thummel, Jared Rutter

Open access · bronzeAbstract read
In one paragraph

Article in Cell metabolism, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

71 citing papers in PubMed, 108 citations in OpenAlex.

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11 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 2 institutions in 1 country.

Jonathan G Van VrankenDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112, USA.
Daniel K BrickerDepartment of Human Genetics, University of Utah School of Medicine, Salt Lake City, UT 84112, USA.
Noah DephoureDepartment of Cell Biology, Harvard University Medical School, Boston, MA 02115, USA.
Steven P GygiDepartment of Cell Biology, Harvard University Medical School, Boston, MA 02115, USA.
James E CoxMetabolomics Core Research Facility, University of Utah School of Medicine, Salt Lake City, UT 84112, USA.
Carl S ThummelDepartment of Human Genetics, University of Utah School of Medicine, Salt Lake City, UT 84112, USA. Electronic address: carl.thummel@genetics.utah.edu.
Jared RutterDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112, USA. Electronic address: rutter@biochem.utah.edu.
University of Utah · USHarvard University · US

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 1986 to 2026
$72.6M
TRAINING PROGRAM IN GENETICST32GM007464 · NIGMS · UNIVERSITY OF UTAH · PI GRUNWALD, DAVID J., STANFIELD, GILLIAN · 1985 to 2020
$6.1M
MULTIDISCIPLINARY CANCER RESEARCH TRAINING PROGRAMT32CA093247 · NCI · UNIVERSITY OF UTAH · PI AYER, DONALD E · 2002 to 2011
$5.2M
Succinate Dehydrogenase: Biogenesis and Role in DiseaseR01GM110755 · NIGMS · UNIVERSITY OF UTAH · PI WINGE, DENNIS R. · 2014 to 2021
$2.3M
Functions of the Mitochondrial Proteome: An Integrated Multi-Species ApproachR01GM094232 · NIGMS · UNIVERSITY OF UTAH · PI RUTTER, JARED P, THUMMEL, CARL S. · 2012 to 2015
$1.2M
NCI NIH HHS P30 CA042014NCI NIH HHS P30CA042014NCI NIH HHS T32 CA093247NIGMS NIH HHS 1R01 GM094232NIGMS NIH HHS 1R01 GM110755NIGMS NIH HHS R01 GM094232NIGMS NIH HHS R01 GM110755NIGMS NIH HHS T32 GM007464
6 · The paper itself

Abstract

Succinate dehydrogenase (SDH) occupies a central place in cellular energy production, linking the tricarboxylic cycle with the electron transport chain. As a result, a subset of cancers and neuromuscular disorders result from mutations affecting any of the four SDH structural subunits or either of two known SDH assembly factors. Herein we characterize an evolutionarily conserved SDH assembly factor designated Sdh8/SDHAF4, using yeast, Drosophila, and mammalian cells. Sdh8 interacts specifically with the catalytic Sdh1 subunit in the mitochondrial matrix, facilitating its association with Sdh2 and the subsequent assembly of the SDH holocomplex. These roles for Sdh8 are critical for preventing motility defects and neurodegeneration in Drosophila as well as the excess ROS generated by free Sdh1. These studies provide insights into the mechanisms by which SDH is assembled and raise the possibility that some forms of neuromuscular disease may be associated with mutations that affect this SDH assembly factor.

Indexed as

AnimalsDrosophilaDrosophila ProteinsElectron Transport Complex IIMaleMiceMitochondriaMitochondrial ProteinsNeurodegenerative DiseasesOxidative StressRNA InterferenceRNA, Small InterferingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSuccinate DehydrogenaseDrosophila ProteinsElectron Transport Complex IIMitochondrial ProteinsRNA, Small InterferingSaccharomyces cerevisiae ProteinsSDH1 protein, S cerevisiaeSuccinate Dehydrogenase

Identifiers

PMID24954416
PMCPMC4126880
OpenAlexW2165904478

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.