Evidence map›Paper›PMID 37845336›Full record

ArticleNature plants2023

ARP2/3 complex associates with peroxisomes to participate in pexophagy in plants.

Jan Martinek, Petra Cifrová, Stanislav Vosolsobě, Judith García-González, Kateřina Malínská, Zdeňka Mauerová, Barbora Jelínková, Jana Krtková, Lenka Sikorová, Ian Leaves and 2 more

Open access · greenAbstract read
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In one paragraph

Article in Nature plants, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

10 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
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  5. The ER-PM interaction is essential for cytokinesis and recruits the actin cytoskeleton through the SCAR/WAVE complex.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

12 authors at 4 institutions in 2 countries.

Jan MartinekDepartment of Experimental Plant Biology, Faculty of Science, Charles University, Prague, Czech Republic.ORCID http://orcid.org/0000-0002-5078-702X
Petra CifrováDepartment of Experimental Plant Biology, Faculty of Science, Charles University, Prague, Czech Republic.
Stanislav VosolsoběDepartment of Experimental Plant Biology, Faculty of Science, Charles University, Prague, Czech Republic.ORCID http://orcid.org/0000-0002-1180-3250
Judith García-GonzálezDepartment of Experimental Plant Biology, Faculty of Science, Charles University, Prague, Czech Republic.ORCID http://orcid.org/0000-0002-3752-4102
Kateřina MalínskáImaging Facility of Institute of Experimental Botany AS CR, Prague, Czech Republic.ORCID http://orcid.org/0000-0002-7928-9825
Zdeňka MauerováDepartment of Experimental Plant Biology, Faculty of Science, Charles University, Prague, Czech Republic.
Barbora JelínkováDepartment of Experimental Plant Biology, Faculty of Science, Charles University, Prague, Czech Republic.
Jana KrtkováDepartment of Experimental Plant Biology, Faculty of Science, Charles University, Prague, Czech Republic.ORCID http://orcid.org/0000-0002-9197-9730
Lenka SikorováDepartment of Experimental Plant Biology, Faculty of Science, Charles University, Prague, Czech Republic.
Ian LeavesBiosciences, CLES, Exeter University, Exeter, UK.ORCID http://orcid.org/0000-0002-5612-9087
Imogen SparkesSchool of Biological Sciences, University of Bristol, Bristol, UK.ORCID http://orcid.org/0000-0001-7789-5074
Kateřina SchwarzerováDepartment of Experimental Plant Biology, Faculty of Science, Charles University, Prague, Czech Republic. schwarze@natur.cuni.cz.ORCID http://orcid.org/0000-0001-5269-9499
Charles University · CZCzech Academy of Sciences, Institute of Experimental Botany · CZUniversity of Bristol · GBUniversity of Exeter · GB

Funding

Grantová Agentura, Univerzita Karlova (Charles University Grant Agency) 374522Grantová Agentura, Univerzita Karlova (Charles University Grant Agency) 816217
6 · The paper itself

Abstract

Actin-related protein (ARP2/3) complex is a heteroheptameric protein complex, evolutionary conserved in all eukaryotic organisms. Its conserved role is based on the induction of actin polymerization at the interface between membranes and the cytoplasm. Plant ARP2/3 has been reported to participate in actin reorganization at the plasma membrane during polarized growth of trichomes and at the plasma membrane-endoplasmic reticulum contact sites. Here we demonstrate that individual plant subunits of ARP2/3 fused to fluorescent proteins form motile spot-like structures in the cytoplasm that are associated with peroxisomes in Arabidopsis and tobacco. ARP2/3 is found at the peroxisome periphery and contains the assembled ARP2/3 complex and the WAVE/SCAR complex subunit NAP1. This ARP2/3-positive peroxisomal domain colocalizes with the autophagosome and, under conditions that affect the autophagy, colocalization between ARP2/3 and the autophagosome increases. ARP2/3 subunits co-immunoprecipitate with ATG8f and peroxisome-associated ARP2/3 interact in vivo with the ATG8f marker. Since mutants lacking functional ARP2/3 complex have more peroxisomes than wild type, we suggest that ARP2/3 has a novel role in the process of peroxisome degradation by autophagy, called pexophagy.

Indexed as

ArabidopsisArabidopsis ProteinsActin-Related Protein 2-3 ComplexActinsMacroautophagyPeroxisomesActin-Related Protein 2-3 ComplexActinsArabidopsis Proteins

Identifiers

PMID37845336
OpenAlexW4387666766

What OpenQuestion holds

Textmetadata
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.