Evidence map›Paper›PMID 42010247›Full record

ArticleNature communications2026

Assembly of two functionally-distinct protein import complexes in the outer membrane of plant chloroplasts.

Sreedhar Nellaepalli, Domagoj Baretić, Astrid F Brandner, Sybille Kubis-Waller, Duorong Xu, Ziad Soufi, Shuyang Cheng, Sireesha Kodru, Jun Fang, Úrsula Flores-Pérez and 6 more

Abstract read
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In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Article
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

16 authors.

Sreedhar Nellaepalli *Section of Molecular Plant Biology, Department of Biology, University of Oxford, Oxford, UK. sreedhar.nellaepalli@biology.ox.ac.uk.ORCID http://orcid.org/0000-0002-9402-6951
Domagoj Baretić *Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-7049-3961
Astrid F BrandnerDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-5023-8127
Sybille Kubis-WallerDepartment of Biology, University of Leicester, Leicester, UK.
Duorong XuSection of Molecular Plant Biology, Department of Biology, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-0566-3722
Ziad SoufiSection of Molecular Plant Biology, Department of Biology, University of Oxford, Oxford, UK.
Shuyang ChengSection of Molecular Plant Biology, Department of Biology, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-5311-7235
Sireesha KodruSection of Molecular Plant Biology, Department of Biology, University of Oxford, Oxford, UK.
Jun FangSection of Molecular Plant Biology, Department of Biology, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0003-2049-3271
Úrsula Flores-PérezSection of Molecular Plant Biology, Department of Biology, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-6780-3671
Vaishnavi RavikumarDepartment of Biochemistry, University of Oxford, Oxford, UK.
Pablo PulidoSection of Molecular Plant Biology, Department of Biology, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-9092-3674
Marjorie FournierDepartment of Biochemistry, University of Oxford, Oxford, UK.
Ivan AhelSir William Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-9446-3756
Syma KhalidDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-3694-5044
R Paul JarvisSection of Molecular Plant Biology, Department of Biology, University of Oxford, Oxford, UK. paul.jarvis@biology.ox.ac.uk.ORCID http://orcid.org/0000-0003-2127-5671

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The TOC translocon delivers thousands of nucleus-encoded proteins to chloroplasts and related non-photosynthetic plastids. It comprises the β-barrel channel, Toc75, and multiple isoforms of receptor GTPases, Toc33 and Toc159. However, exactly how TOC complexes are assembled in different plastid types is unknown. Here, we present detailed characterisation of two distinct TOC complexes, TOC-P and TOC-N, from photosynthetic chloroplasts and non-photosynthetic plastids, respectively. The assembled complexes are distinguished by having different sets of receptors, but both possess Toc75 which we identify as a central hub in TOC biogenesis: assembly is driven by TOC75 expression, with Toc33 and Toc159 being added sequentially thereafter. Integrative structural analysis reveals a modular architecture for TOC-P comprising a cytosolic GTPase receptor module linked flexibly to a membrane β-barrel channel module. TOC-N has a similar overall architecture, albeit with some clear differences that likely account for observed functional differences related to client specificity.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplastsIntracellular MembranesMembrane ProteinsGTP PhosphohydrolasesProtein PrecursorsProtein TransportArabidopsis ProteinsGTP PhosphohydrolasesMembrane ProteinsProtein PrecursorsTOC159 protein, ArabidopsisToc33 protein, ArabidopsisTOC75 protein, Arabidopsis

Identifiers

PMID42010247
PMCPMC13279931

What Socratic 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 Socratic graph.