Evidence map›Paper›PMID 31911454›Full record

ReviewThe Plant cell2020

Matrix Redox Physiology Governs the Regulation of Plant Mitochondrial Metabolism through Posttranslational Protein Modifications.

Ian Max Møller, Abir U Igamberdiev, Natalia V Bykova, Iris Finkemeier, Allan G Rasmusson, Markus Schwarzländer

Open access · bronzeAbstract readReview
In one paragraph

Review in The Plant cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 84 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 5 institutions in 4 countries.

Ian Max MøllerDepartment of Molecular Biology and Genetics, Aarhus University, DK-4200 Slagelse, Denmark ian.max.moller@mbg.au.dk.ORCID 0000-0002-7919-7787
Abir U IgamberdievDepartment of Biology, Memorial University of Newfoundland, St. John's, Newfoundland A1B 3X9, Canada.ORCID 0000-0002-7253-607X
Natalia V BykovaAgriculture and Agri-Food Canada, Morden Research and Development Centre, Morden, Manitoba R6M 1Y5, Canada.ORCID 0000-0002-5482-3251
Iris FinkemeierInstitute of Plant Biology and Biotechnology, University of Münster, DE-48149 Münster, Germany.ORCID 0000-0002-8972-4026
Allan G RasmussonDepartment of Biology, Lund University, SE-22362 Lund, Sweden.ORCID 0000-0003-0734-5020
Markus SchwarzländerInstitute of Plant Biology and Biotechnology, University of Münster, DE-48143 Münster, Germany.ORCID 0000-0003-0796-8308
University of Münster · DEAarhus University · DKAgriculture and Agri-Food Canada · CALund University · SEMemorial University of Newfoundland · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria function as hubs of plant metabolism. Oxidative phosphorylation produces ATP, but it is also a central high-capacity electron sink required by many metabolic pathways that must be flexibly coordinated and integrated. Here, we review the crucial roles of redox-associated posttranslational protein modifications (PTMs) in mitochondrial metabolic regulation. We discuss several major concepts. First, the major redox couples in the mitochondrial matrix (NAD, NADP, thioredoxin, glutathione, and ascorbate) are in kinetic steady state rather than thermodynamic equilibrium. Second, targeted proteomics have produced long lists of proteins potentially regulated by Cys oxidation/thioredoxin, Met-SO formation, phosphorylation, or Lys acetylation, but we currently only understand the functional importance of a few of these PTMs. Some site modifications may represent molecular noise caused by spurious reactions. Third, different PTMs on the same protein or on different proteins in the same metabolic pathway can interact to fine-tune metabolic regulation. Fourth, PTMs take part in the repair of stress-induced damage (e.g., by reducing Met and Cys oxidation products) as well as adjusting metabolic functions in response to environmental variation, such as changes in light irradiance or oxygen availability. Finally, PTMs form a multidimensional regulatory system that provides the speed and flexibility needed for mitochondrial coordination far beyond that provided by changes in nuclear gene expression alone.

Indexed as

Protein Processing, Post-TranslationalGerminationMitochondriaMitochondrial ProteinsOxidation-ReductionPlantsMitochondrial Proteins

Identifiers

PMID31911454
PMCPMC7054041
OpenAlexW3000335848

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.