Evidence map›Paper›PMID 37721949›Full record

ArticlePLoS biology2023

SEC14-like condensate phase transitions at plasma membranes regulate root growth in Arabidopsis.

Chen Liu, Andriani Mentzelopoulou, Fotini Papagavriil, Prashanth Ramachandran, Artemis Perraki, Lucas Claus, Sebastian Barg, Peter Dörmann, Yvon Jaillais, Philipp Johnen and 4 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PLoS biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
9.1field-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

16 citing papers in PubMed, 23 citations in OpenAlex.

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  12. Exploring lipid-protein interactions in plant membranes.Journal of experimental botany · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 6 institutions in 5 countries.

Chen LiuDepartment of Biology, University of Crete, Heraklion, Greece.
Andriani MentzelopoulouDepartment of Biology, University of Crete, Heraklion, Greece.
Fotini PapagavriilDepartment of Biology, University of Crete, Heraklion, Greece.
Prashanth RamachandranDepartment of Organismal Biology, Physiological Botany, Linnean Centre for Plant Biology, Uppsala University, Uppsala, Sweden.
Artemis PerrakiInstitute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas, Heraklion, Greece.
Lucas ClausDepartment of Plant Biotechnology and Bioinformatics, Ghent University, Ghent, Belgium.
Sebastian BargDepartment of Medical Cell Biology, Uppsala University, Uppsala, Sweden.
Peter DörmannInstitute of Molecular Physiology and Biotechnology of Plants, University of Bonn, Bonn, Germany.
Yvon JaillaisLaboratoire Reproduction et Développement des Plantes, ENS de Lyon, Université Claude Bernard Lyon 1, CNRS, INRAE, Lyon, France.
Philipp JohnenDepartment of Plant Nutrition, Institute of Crop Science and Resource Conservation, University of Bonn, Bonn, Germany.
Eugenia RussinovaDepartment of Plant Biotechnology and Bioinformatics, Ghent University, Ghent, Belgium.
Electra GizeliDepartment of Biology, University of Crete, Heraklion, Greece.
Gabriel SchaafDepartment of Plant Nutrition, Institute of Crop Science and Resource Conservation, University of Bonn, Bonn, Germany.
Panagiotis Nikolaou MoschouDepartment of Biology, University of Crete, Heraklion, Greece.ORCID https://orcid.org/0000-0001-7212-0595
University of Crete · GRUniversity of Bonn · DEGhent University · BEUppsala University · SEFoundation for Research and Technology Hellas · GRUniversité Claude Bernard Lyon 1 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein function can be modulated by phase transitions in their material properties, which can range from liquid- to solid-like; yet, the mechanisms that drive these transitions and whether they are important for physiology are still unknown. In the model plant Arabidopsis, we show that developmental robustness is reinforced by phase transitions of the plasma membrane-bound lipid-binding protein SEC14-like. Using imaging, genetics, and in vitro reconstitution experiments, we show that SEC14-like undergoes liquid-like phase separation in the root stem cells. Outside the stem cell niche, SEC14-like associates with the caspase-like protease separase and conserved microtubule motors at unique polar plasma membrane interfaces. In these interfaces, SEC14-like undergoes processing by separase, which promotes its liquid-to-solid transition. This transition is important for root development, as lines expressing an uncleavable SEC14-like variant or mutants of separase and associated microtubule motors show similar developmental phenotypes. Furthermore, the processed and solidified but not the liquid form of SEC14-like interacts with and regulates the polarity of the auxin efflux carrier PINFORMED2. This work demonstrates that robust development can involve liquid-to-solid transitions mediated by proteolysis at unique plasma membrane interfaces.

Identifiers

PMID37721949
PMCPMC10538751
OpenAlexW4386825725

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.