Evidence map›Paper›PMID 31676684›Full record

ArticleThe Journal of biological chemistry2019

Multiple mitochondrial thioesterases have distinct tissue and substrate specificity and CoA regulation, suggesting unique functional roles.

Carmen Bekeova, Lauren Anderson-Pullinger, Kevin Boye, Felix Boos, Yana Sharpadskaya, Johannes M Herrmann, Erin L Seifert

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 1 synthesis or guideline pooled it, 40 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.

Carmen BekeovaMitoCare Center, Department of Pathology, Anatomy, and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
Lauren Anderson-PullingerMitoCare Center, Department of Pathology, Anatomy, and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
Kevin BoyeMitoCare Center, Department of Pathology, Anatomy, and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
Felix BoosDivision of Cellular Biology, Department of Biology, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
Yana SharpadskayaMitoCare Center, Department of Pathology, Anatomy, and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
Johannes M HerrmannDivision of Cellular Biology, Department of Biology, University of Kaiserslautern, 67663 Kaiserslautern, Germany.ORCID 0000-0003-2081-4506
Erin L SeifertMitoCare Center, Department of Pathology, Anatomy, and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107 erin.seifert@jefferson.edu.ORCID 0000-0002-8416-5763
Thomas Jefferson University · USUniversity of Kaiserslautern · DE

Funding

Regulation of substrate metabolism in skeletal muscle by mitochondrial thioesterasesR01DK109100 · NIDDK · THOMAS JEFFERSON UNIVERSITY · PI SEIFERT, ERIN · 2017 to 2020
$1.6M
NIDDK NIH HHS R01 DK109100
6 · The paper itself

Abstract

Acyl-CoA thioesterases (Acots) hydrolyze fatty acyl-CoA esters. Acots in the mitochondrial matrix are poised to mitigate β-oxidation overload and maintain CoA availability. Several Acots associate with mitochondria, but whether they all localize to the matrix, are redundant, or have different roles is unresolved. Here, we compared the suborganellar localization, activity, expression, and regulation among mitochondrial Acots (Acot2, -7, -9, and -13) in mitochondria from multiple mouse tissues and from a model of Acot2 depletion. Acot7, -9, and -13 localized to the matrix, joining Acot2 that was previously shown to localize there. Mitochondria from heart, skeletal muscle, brown adipose tissue, and kidney robustly expressed Acot2, -9, and -13; Acot9 levels were substantially higher in brown adipose tissue and kidney mitochondria, as was activity for C4:0-CoA, a unique Acot9 substrate. In all tissues, Acot2 accounted for about half of the thioesterase activity for C14:0-CoA and C16:0-CoA. In contrast, liver mitochondria from fed and fasted mice expressed little Acot activity, which was confined to long-chain CoAs and due mainly to Acot7 and Acot13 activities. Matrix Acots occupied different functional niches, based on substrate specificity (Acot9

Indexed as

Acyl Coenzyme AAnimalsMaleMiceMice, Inbred C57BLMice, KnockoutMitochondriaPalmitoyl-CoA HydrolaseRecombinant ProteinsSubstrate SpecificityThiolester HydrolasesAcot13 protein, mouseAcot7 protein, mouseAcyl Coenzyme Amitochondrial acyl-CoA thioesterase I, mousePalmitoyl-CoA HydrolaseRecombinant ProteinsThiolester Hydrolasesacyl-CoA thioesterase (Acot)allosteric regulationcoenzyme A (CoA)enzyme compartmentalizationfatty acid oxidationlipid hydrolaselipid metabolismlong-chain acyl-CoA regulationmitochondriamitochondrial matrixmitochondrial metabolismmousesubcellular localization

Identifiers

PMID31676684
PMCPMC6916504
OpenAlexW2985889236

What OpenQuestion holds

Textmetadata
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.