Evidence map›Paper›PMID 36741000›Full record

ArticleThe EMBO journal2023

An actin remodeling role for Arabidopsis processing bodies revealed by their proximity interactome.

Chen Liu, Andriani Mentzelopoulou, Amna Muhammad, Andriy Volkov, Dolf Weijers, Emilio Gutierrez-Beltran, Panagiotis N Moschou

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

30 citing papers in PubMed, 33 citations in OpenAlex.

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  17. 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

7 authors at 5 institutions in 5 countries.

Chen LiuDepartment of Plant Biology, Uppsala BioCenter, Swedish University of Agricultural Sciences and Linnean Center for Plant Biology, Uppsala, Sweden.ORCID 0000-0002-1604-0694
Andriani MentzelopoulouDepartment of Biology, University of Crete, Heraklion, Greece.ORCID 0000-0003-4266-8714
Amna MuhammadDepartment of Plant Biology, Uppsala BioCenter, Swedish University of Agricultural Sciences and Linnean Center for Plant Biology, Uppsala, Sweden.
Andriy VolkovLaboratory of Biochemistry, Wageningen University and Research, Wageningen, The Netherlands.
Dolf WeijersLaboratory of Biochemistry, Wageningen University and Research, Wageningen, The Netherlands.ORCID 0000-0003-4378-141X
Emilio Gutierrez-BeltranInstituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla and Consejo Superior de Investigaciones Científicas, Seville, Spain.ORCID 0000-0001-7978-3164
Panagiotis N MoschouDepartment of Plant Biology, Uppsala BioCenter, Swedish University of Agricultural Sciences and Linnean Center for Plant Biology, Uppsala, Sweden.ORCID 0000-0001-7212-0595
University of Crete · GRWageningen University & Research · NLConsejo Superior de Investigaciones Científicas · ESPir Mehr Ali Shah Arid Agriculture University · PKSwedish University of Agricultural Sciences · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular condensates can comprise membrane-less ribonucleoprotein assemblies with liquid-like properties. These cellular condensates influence various biological outcomes, but their liquidity hampers their isolation and characterization. Here, we investigated the composition of the condensates known as processing bodies (PBs) in the model plant Arabidopsis thaliana through a proximity-biotinylation proteomics approach. Using in situ protein-protein interaction approaches, genetics and high-resolution dynamic imaging, we show that processing bodies comprise networks that interface with membranes. Surprisingly, the conserved component of PBs, DECAPPING PROTEIN 1 (DCP1), can localize to unique plasma membrane subdomains including cell edges and vertices. We characterized these plasma membrane interfaces and discovered a developmental module that can control cell shape. This module is regulated by DCP1, independently from its role in decapping, and the actin-nucleating SCAR-WAVE complex, whereby the DCP1-SCAR-WAVE interaction confines and enhances actin nucleation. This study reveals an unexpected function for a conserved condensate at unique membrane interfaces.

Indexed as

ActinsArabidopsisArabidopsis ProteinsActin-Related Protein 2-3 ComplexProcessing BodiesActin-Related Protein 2-3 ComplexActinsArabidopsis ProteinsARP2-ARP3condensatesLLPSplasma membrane domainsSCAR-WAVE

Identifiers

PMID36741000
PMCPMC10152145
OpenAlexW4319294326

What OpenQuestion holds

Textmetadata
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.