Evidence map›Paper›PMID 34588454›Full record

ArticleNature communications2021

Mapping protein interactions in the active TOM-TIM23 supercomplex.

Ridhima Gomkale, Andreas Linden, Piotr Neumann, Alexander Benjamin Schendzielorz, Stefan Stoldt, Olexandr Dybkov, Markus Kilisch, Christian Schulz, Luis Daniel Cruz-Zaragoza, Blanche Schwappach and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

37 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
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  3. Mass spectrometry proteomics for studying mitostasis.Protein science : a publication of the Protein Society · 2026
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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 4 institutions in 1 country.

Ridhima GomkaleDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.ORCID 0000-0003-0897-1365
Andreas LindenDepartment of Clinical Chemistry, University Medical Center Göttingen, Göttingen, Germany.ORCID 0000-0002-6365-1164
Piotr NeumannDepartment for Molecular Structural Biology, Georg-August-Universität Göttingen, Göttingen, Germany.ORCID 0000-0003-0129-8112
Alexander Benjamin SchendzielorzDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Stefan StoldtDepartment of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Olexandr DybkovCellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen, Germany.ORCID 0000-0001-6005-7242
Markus KilischDepartment of Molecular Biology, University Medical Center Göttingen, Göttingen, Germany.
Christian SchulzDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Luis Daniel Cruz-ZaragozaDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.ORCID 0000-0001-9568-0245
Blanche SchwappachDepartment of Molecular Biology, University Medical Center Göttingen, Göttingen, Germany.ORCID 0000-0003-0225-6432
Ralf FicnerDepartment for Molecular Structural Biology, Georg-August-Universität Göttingen, Göttingen, Germany.ORCID 0000-0002-1739-6086
Stefan JakobsDepartment of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0002-8028-3121
Henning UrlaubDepartment of Clinical Chemistry, University Medical Center Göttingen, Göttingen, Germany.ORCID 0000-0003-1837-5233
Peter RehlingDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany. peter.rehling@medizin.uni-goettingen.de.ORCID 0000-0001-5661-5272
Universitätsmedizin Göttingen · DEMax Planck Institute for Biophysical Chemistry · DENanoscale Microscopy and Molecular Physiology of the Brain Cluster of Excellence 171 — DFG Research Center 103 · DEUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclear-encoded mitochondrial proteins destined for the matrix have to be transported across two membranes. The TOM and TIM23 complexes facilitate the transport of precursor proteins with N-terminal targeting signals into the matrix. During transport, precursors are recognized by the TIM23 complex in the inner membrane for handover from the TOM complex. However, we have little knowledge on the organization of the TOM-TIM23 transition zone and on how precursor transfer between the translocases occurs. Here, we have designed a precursor protein that is stalled during matrix transport in a TOM-TIM23-spanning manner and enables purification of the translocation intermediate. Combining chemical cross-linking with mass spectrometric analyses and structural modeling allows us to map the molecular environment of the intermembrane space interface of TOM and TIM23 as well as the import motor interactions with amino acid resolution. Our analyses provide a framework for understanding presequence handover and translocation during matrix protein transport.

Indexed as

Cell FractionationCell NucleusCross-Linking ReagentsMass SpectrometryMembrane Transport ProteinsMitochondriaMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMolecular Docking SimulationMutagenesis, Site-DirectedPoint MutationProtein BindingProtein Interaction MappingProtein PrecursorsRecombinant ProteinsCross-Linking ReagentsMembrane Transport ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsProtein PrecursorsRecombinant ProteinsSaccharomyces cerevisiae ProteinsTIM23 protein, S cerevisiaeTIM44 protein, S cerevisiae

Identifiers

PMID34588454
PMCPMC8481542
OpenAlexW3204781979

What OpenQuestion holds

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LicenceCC BY
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.