Evidence map›Paper›PMID 29802333›Full record

ArticleScientific reports2018

Insight into the fission mechanism by quantitative characterization of Drp1 protein distribution in the living cell.

Bernadeta Maria Michalska, Karina Kwapiszewska, Joanna Szczepanowska, Tomasz Kalwarczyk, Paulina Patalas-Krawczyk, Krzysztof Szczepański, Robert Hołyst, Jerzy Duszyński, Jędrzej Szymański

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.7field-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

36 citing papers in PubMed, 43 citations in OpenAlex.

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  11. Alternative splice variants of the mitochondrial fission proteinbioRxiv : the preprint server for biology · 2024
    Article
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  17. Converging Role for REEP1/SPG31 in Oxidative Stress.International journal of molecular sciences · 2023
    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

9 authors at 2 institutions in 1 country.

Bernadeta Maria MichalskaLaboratory of Bioenergetics and Biomembranes, Department of Biochemistry, Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur Str, 02-093, Warsaw, Poland.
Karina KwapiszewskaInstitute of Physical Chemistry, Polish Academy of Sciences, Kasprzaka 44/52, 01-224, Warsaw, Poland.ORCID 0000-0002-7396-9571
Joanna SzczepanowskaLaboratory of Bioenergetics and Biomembranes, Department of Biochemistry, Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur Str, 02-093, Warsaw, Poland.
Tomasz KalwarczykInstitute of Physical Chemistry, Polish Academy of Sciences, Kasprzaka 44/52, 01-224, Warsaw, Poland.
Paulina Patalas-KrawczykLaboratory of Bioenergetics and Biomembranes, Department of Biochemistry, Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur Str, 02-093, Warsaw, Poland.
Krzysztof SzczepańskiInstitute of Physical Chemistry, Polish Academy of Sciences, Kasprzaka 44/52, 01-224, Warsaw, Poland.
Robert HołystInstitute of Physical Chemistry, Polish Academy of Sciences, Kasprzaka 44/52, 01-224, Warsaw, Poland.
Jerzy DuszyńskiLaboratory of Bioenergetics and Biomembranes, Department of Biochemistry, Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur Str, 02-093, Warsaw, Poland.
Jędrzej SzymańskiLaboratory of Bioenergetics and Biomembranes, Department of Biochemistry, Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur Str, 02-093, Warsaw, Poland. j.szymanski@nencki.gov.pl.ORCID 0000-0002-4060-0196
Instytut Biologii Doświadczalnej im. Marcelego Nenckiego · PLInstitute of Physical Chemistry · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One of the main players in the process of mitochondrial fragmentation is dynamin-related protein 1 (Drp1), which assembles into a helical ring-like structure on the mitochondria and facilitates fission. The fission mechanism is still poorly understood and detailed information concerning oligomeric form of Drp1, its cellular distribution and the size of the fission complex is missing. To estimate oligomeric forms of Drp1 in the cytoplasm and on the mitochondria, we performed a quantitative analysis of Drp1 diffusion and distribution in gene-edited HeLa cell lines. This paper provides an insight into the fission mechanism based on the quantitative description of Drp1 cellular distribution. We found that approximately half of the endogenous GFP-Drp1 pool remained in the cytoplasm, predominantly in a tetrameric form, at a concentration of 28 ± 9 nM. The Drp1 mitochondrial pool included many different oligomeric states with equilibrium distributions that could be described by isodesmic supramolecular polymerization with a K

Indexed as

Cell SurvivalCytoplasmDynaminsGTP PhosphohydrolasesHeLa CellsHumansMicrotubule-Associated ProteinsMitochondriaMitochondrial ProteinsModels, MolecularProtein MultimerizationProtein Structure, QuaternaryProtein TransportViscosityDNM1L protein, humanDynaminsGTP PhosphohydrolasesMicrotubule-Associated ProteinsMitochondrial Proteins

Identifiers

PMID29802333
PMCPMC5970238
OpenAlexW2803890843

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.