Evidence map›Paper›PMID 33177075›Full record

ArticleJournal of cell science2020

A piggybacking mechanism enables peroxisomal localization of the glyoxylate cycle enzyme Mdh2 in yeast.

Shiran Gabay-Maskit, Luis Daniel Cruz-Zaragoza, Nadav Shai, Miriam Eisenstein, Chen Bibi, Nir Cohen, Tobias Hansen, Eden Yifrach, Nofar Harpaz, Ruth Belostotsky and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 33 citations in OpenAlex.

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  15. Translating theFrontiers in cell and developmental biology · 2022
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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

14 authors at 3 institutions in 2 countries.

Shiran Gabay-MaskitDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Luis Daniel Cruz-ZaragozaAbteilung für Systembiochemie, Institut für Biochemie und Pathobiochemie, Medizinische Fakultät, Ruhr-Universität Bochum, Bochum D-44780, Germany.
Nadav ShaiDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.ORCID 0000-0002-2812-3884
Miriam EisensteinDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Chen BibiDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Nir CohenDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Tobias HansenAbteilung für Systembiochemie, Institut für Biochemie und Pathobiochemie, Medizinische Fakultät, Ruhr-Universität Bochum, Bochum D-44780, Germany.
Eden YifrachDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Nofar HarpazDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Ruth BelostotskyDivision of Pediatric Nephrology, Shaare Zedek Medical Center, Jerusalem, Israel.
Wolfgang SchliebsAbteilung für Systembiochemie, Institut für Biochemie und Pathobiochemie, Medizinische Fakultät, Ruhr-Universität Bochum, Bochum D-44780, Germany.
Maya SchuldinerDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel maya.schuldiner@weizmann.ac.il ralf.erdmann@rub.de einat.zalckvar@weizmann.ac.il.ORCID 0000-0001-9947-115X
Ralf ErdmannAbteilung für Systembiochemie, Institut für Biochemie und Pathobiochemie, Medizinische Fakultät, Ruhr-Universität Bochum, Bochum D-44780, Germany maya.schuldiner@weizmann.ac.il ralf.erdmann@rub.de einat.zalckvar@weizmann.ac.il.ORCID 0000-0001-8380-0342
Einat ZalckvarDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel maya.schuldiner@weizmann.ac.il ralf.erdmann@rub.de einat.zalckvar@weizmann.ac.il.ORCID 0000-0003-3724-3965
Weizmann Institute of Science · ILRuhr University Bochum · DEShaare Zedek Medical Center · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic cells have evolved organelles that allow the compartmentalization and regulation of metabolic processes. Knowledge of molecular mechanisms that allow temporal and spatial organization of enzymes within organelles is therefore crucial for understanding eukaryotic metabolism. Here, we show that the yeast malate dehydrogenase 2 (Mdh2) is dually localized to the cytosol and to peroxisomes and is targeted to peroxisomes via association with Mdh3 and a Pex5-dependent piggybacking mechanism. This dual localization of Mdh2 contributes to our understanding of the glyoxylate cycle and provides a new perspective on compartmentalization of cellular metabolism, which is critical for the perception of metabolic disorders and aging.

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmino Acid SequenceCytosolGlyoxylatesMalate DehydrogenasePeroxisomesGlyoxylatesMalate DehydrogenaseMDH2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsGlyoxylate cycleMalate dehydrogenasePeroxisomesPex5PiggybackingProtein targeting

Identifiers

PMID33177075
PMCPMC7758625
OpenAlexW3105710228

What OpenQuestion holds

Textmetadata
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.