Evidence map›Paper›PMID 39160348›Full record

ArticleNature plants2024

Recruitment of Cdc48 to chloroplasts by a UBX-domain protein in chloroplast-associated protein degradation.

Na Li, R Paul Jarvis

Abstract read
In one paragraph

Article in Nature plants, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
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  4. Review
  5. Proteolytic control of mitochondrial protein translocases.Protein science : a publication of the Protein Society · 2026
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Na LiSection of Molecular Plant Biology, Department of Biology, University of Oxford, Oxford, UK.
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

RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/K018442/1, BB/N006372/1, BB/R016984/1, BB/R009333/1, BB/V007300/1, BB/W015021/1, and BB/X000192/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) Interdisciplinary Bioscience Doctoral Training Partnership
6 · The paper itself

Abstract

The translocon at the outer chloroplast membrane (TOC) is the gateway for chloroplast protein import and so is vital for photosynthetic establishment and plant growth. Chloroplast-associated protein degradation (CHLORAD) is a ubiquitin-dependent proteolytic system that regulates TOC. In CHLORAD, cytosolic Cdc48 provides motive force for the retrotranslocation of ubiquitinated TOC proteins to the cytosol but how Cdc48 is recruited is unknown. Here, we identify plant UBX-domain protein PUX10 as a component of the CHLORAD machinery. We show that PUX10 is an integral chloroplast outer membrane protein that projects UBX and ubiquitin-associated domains into the cytosol. It interacts with Cdc48 via its UBX domain, bringing it to the chloroplast surface, and with ubiquitinated TOC proteins via its ubiquitin-associated domain. Genetic analyses in Arabidopsis revealed a requirement for PUX10 during CHLORAD-mediated regulation of TOC function and plant development. Thus, PUX10 coordinates ubiquitination and retrotranslocation activities of CHLORAD to enable efficient TOC turnover.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplastsProteolysisChloroplast ProteinsProtein DomainsUbiquitinationValosin Containing ProteinArabidopsis ProteinsChloroplast ProteinsValosin Containing Protein

Identifiers

PMID39160348
PMCPMC11410653

What OpenQuestion holds

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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.