Evidence map›Paper›PMID 25428986›Full record

ArticleMolecular biology of the cell2015

Methionine sulfoxide reductase 2 reversibly regulates Mge1, a cochaperone of mitochondrial Hsp70, during oxidative stress.

Praveen Kumar Allu, Adinarayana Marada, Yerranna Boggula, Srinivasu Karri, Thanuja Krishnamoorthy, Naresh Babu V Sepuri

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 31 citations in OpenAlex.

  1. Redox signals and oxidative stress in the control of mitochondrial protein import.Protein science : a publication of the Protein Society · 2026
    Review
  2. Review
  3. Article
  4. Treatment of chemotherapy-induced cachexia with BST204: a multimodal validation study.Metabolomics : Official journal of the Metabolomic Society · 2021
    Article
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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.

Praveen Kumar AlluDepartment of Biochemistry, School of Life Sciences, University of Hyderabad, Gachibowli, Hyderabad 500046, India.
Adinarayana MaradaDepartment of Biochemistry, School of Life Sciences, University of Hyderabad, Gachibowli, Hyderabad 500046, India.
Yerranna BoggulaDepartment of Biochemistry, School of Life Sciences, University of Hyderabad, Gachibowli, Hyderabad 500046, India.
Srinivasu KarriDepartment of Biochemistry, School of Life Sciences, University of Hyderabad, Gachibowli, Hyderabad 500046, India.
Thanuja KrishnamoorthyDepartment of Biochemistry, School of Life Sciences, University of Hyderabad, Gachibowli, Hyderabad 500046, India.
Naresh Babu V SepuriDepartment of Biochemistry, School of Life Sciences, University of Hyderabad, Gachibowli, Hyderabad 500046, India nareshuohyd@gmail.com nbvssl@uohyd.ernet.in.
University of Hyderabad · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptide methionine sulfoxide reductases are conserved enzymes that reduce oxidized methionines in protein(s). Although these reductases have been implicated in several human diseases, there is a dearth of information on the identity of their physiological substrates. By using Saccharomyces cerevisiae as a model, we show that of the two methionine sulfoxide reductases (MXR1, MXR2), deletion of mitochondrial MXR2 renders yeast cells more sensitive to oxidative stress than the cytosolic MXR1. Our earlier studies showed that Mge1, an evolutionarily conserved nucleotide exchange factor of Hsp70, acts as an oxidative sensor to regulate mitochondrial Hsp70. In the present study, we show that Mxr2 regulates Mge1 by selectively reducing MetO at position 155 and restores the activity of Mge1 both in vitro and in vivo. Mge1 M155L mutant rescues the slow-growth phenotype and aggregation of proteins of mxr2Δ strain during oxidative stress. By identifying the first mitochondrial substrate for Mxrs, we add a new paradigm to the regulation of the oxidative stress response pathway.

Indexed as

Oxidative StressHSP70 Heat-Shock ProteinsMethionineMethionine Sulfoxide ReductasesMitochondriaMitochondrial Membrane Transport ProteinsMolecular ChaperonesMutant ProteinsOxidation-ReductionOxidoreductasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHSP70 Heat-Shock ProteinsMethionineMethionine Sulfoxide ReductasesMGE1 protein, S cerevisiaeMitochondrial Membrane Transport ProteinsMolecular ChaperonesMutant ProteinsMXR2 protein, S cerevisiaeOxidoreductasesSaccharomyces cerevisiae ProteinsSSA3 protein, S cerevisiae

Identifiers

PMID25428986
PMCPMC4310733
OpenAlexW2129787233

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.