Evidence map›Paper›PMID 24204967›Full record

ArticlePloS one2013

Mmi1, the yeast homologue of mammalian TCTP, associates with stress granules in heat-shocked cells and modulates proteasome activity.

Mark Rinnerthaler, Renata Lejskova, Tomas Grousl, Vendula Stradalova, Gino Heeren, Klaus Richter, Lore Breitenbach-Koller, Jan Malinsky, Jiri Hasek, Michael Breitenbach

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

20 citing papers in PubMed, 34 citations in OpenAlex.

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  12. Behead and live long or the tale of cathepsin L.Yeast (Chichester, England) · 2018
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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

10 authors at 3 institutions in 2 countries.

Mark RinnerthalerDepartment Cell Biology, Division Genetics, University of Salzburg, Salzburg, Austria.
Renata Lejskova
Tomas Grousl
Vendula Stradalova
Gino Heeren
Klaus Richter
Lore Breitenbach-Koller
Jan Malinsky
Jiri Hasek
Michael Breitenbach
University of Salzburg · ATCzech Academy of Sciences, Institute of Microbiology · CZCzech Academy of Sciences, Institute of Experimental Medicine · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As we have shown previously, yeast Mmi1 protein translocates from the cytoplasm to the outer surface of mitochondria when vegetatively growing yeast cells are exposed to oxidative stress. Here we analyzed the effect of heat stress on Mmi1 distribution. We performed domain analyses and found that binding of Mmi1 to mitochondria is mediated by its central alpha-helical domain (V-domain) under all conditions tested. In contrast, the isolated N-terminal flexible loop domain of the protein always displays nuclear localization. Using immunoelectron microscopy we confirmed re-location of Mmi1 to the nucleus and showed association of Mmi1 with intact and heat shock-altered mitochondria. We also show here that mmi1Δ mutant strains are resistant to robust heat shock with respect to clonogenicity of the cells. To elucidate this phenotype we found that the cytosolic Mmi1 holoprotein re-localized to the nucleus even in cells heat-shocked at 40°C. Upon robust heat shock at 46°C, Mmi1 partly co-localized with the proteasome marker Rpn1 in the nuclear region as well as with the cytoplasmic stress granules defined by Rpg1 (eIF3a). We co-localized Mmi1 also with Bre5, Ubp3 and Cdc48 which are involved in the protein de-ubiquitination machinery, protecting protein substrates from proteasomal degradation. A comparison of proteolytic activities of wild type and mmi1Δ cells revealed that Mmi1 appears to be an inhibitor of the proteasome. We conclude that one of the physiological functions of the multifunctional protein module, Mmi1, is likely in regulating degradation and/or protection of proteins thereby indirectly regulating the pathways leading to cell death in stressed cells.

Indexed as

Heat-Shock ResponseAdenosine TriphosphatasesCalcium-Binding ProteinsCell Cycle ProteinsCell NucleusCytoplasmic GranulesEndopeptidasesHot TemperatureMicroscopy, ElectronMicroscopy, FluorescenceProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinValosin Containing ProteinAdenosine TriphosphatasesBre5 protein, S cerevisiaeCalcium-Binding ProteinsCDC48 protein, S cerevisiaeCell Cycle ProteinsEndopeptidasesProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsTMA19 protein, S cerevisiaeUbiquitinUBP3 protein, S cerevisiaeValosin Containing Protein

Identifiers

PMID24204967
PMCPMC3810133
OpenAlexW2014577103

What OpenQuestion holds

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LicenceCC BY
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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.