Evidence map›Paper›PMID 32923632›Full record

ArticleScience advances2020

Cardiolipin, conformation, and respiratory complex-dependent oligomerization of the major mitochondrial ADP/ATP carrier in yeast.

N Senoo, S Kandasamy, O B Ogunbona, M G Baile, Y Lu, S M Claypool

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.6field-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

33 citing papers in PubMed, 47 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

6 authors at 1 institution in 1 country.

N SenooDepartment of Physiology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0001-5260-3848
S KandasamyDepartment of Physiology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0003-0868-6134
O B OgunbonaDepartment of Physiology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0001-5116-7204
M G BaileDepartment of Physiology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0002-2680-1178
Y LuDepartment of Physiology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0003-0479-1471
S M ClaypoolDepartment of Physiology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0001-5316-1623
Johns Hopkins University · US

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
Cardiolipin and the mitochondrial ADP/ATP carrier interactomeR01HL108882 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI CLAYPOOL, STEVEN MICHAEL · 2013 to 2017
$2.0M
NHLBI NIH HHS R01 HL108882NIGMS NIH HHS T32 GM007445
6 · The paper itself

Abstract

The phospholipid cardiolipin has pleiotropic structural and functional roles that are collectively essential for mitochondrial biology. Yet, the molecular details of how this lipid supports the structure and function of proteins and protein complexes are poorly understood. To address this property of cardiolipin, we use the mitochondrial adenosine 5'-diphosphate/adenosine 5'-triphosphate carrier (Aac) as a model. Here, we have determined that cardiolipin is critical for both the tertiary and quaternary assembly of the major yeast Aac isoform Aac2 as well as its conformation. Notably, these cardiolipin-provided structural roles are separable. In addition, we show that multiple copies of Aac2 engage in shared complexes that are largely dependent on the presence of assembled respiratory complexes III and IV or respiratory supercomplexes. Intriguingly, the assembly state of Aac2 is sensitive to its transport-related conformation. Together, these results expand our understanding of the numerous structural roles provided by cardiolipin for mitochondrial membrane proteins.

Indexed as

Mitochondrial ADP, ATP TranslocasesSaccharomyces cerevisiaeAdenosineAdenosine DiphosphateAdenosine TriphosphateCardiolipinsAdenosineAdenosine DiphosphateAdenosine TriphosphateCardiolipinsMitochondrial ADP, ATP Translocases

Identifiers

PMID32923632
PMCPMC7455186
OpenAlexW3081554352

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.