Evidence map›Paper›PMID 40999735›Full record

ReviewThe New phytologist2025

The role of post-translational modifications in the dynamics of cytoplasmic biomolecular condensates in plants.

Margaux Legoux, Jean-Philippe Reichheld, Rémy Merret

Abstract readReview
In one paragraph

Review in The New phytologist, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Molecular basis for thermoresponsive protein condensation in plants.bioRxiv : the preprint server for biology · 2025
    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

3 authors.

Margaux LegouxCNRS-LGDP UMR 5096, 58 Avenue Paul Alduy, 66860, Perpignan, France.ORCID https://orcid.org/0009-0008-1630-6860
Jean-Philippe ReichheldCNRS-LGDP UMR 5096, 58 Avenue Paul Alduy, 66860, Perpignan, France.ORCID https://orcid.org/0000-0001-6884-0602
Rémy MerretIBMP UPR 2357, 23 rue Général Zimmer, 67000, Strasbourg, France.ORCID https://orcid.org/0000-0002-3790-1115

Funding

Agence Nationale de la Recherche ANR-10-LABX-41Agence Nationale de la Recherche ANR-18-EURE-0019Agence Nationale de la Recherche ANR-19-CE12-0027Agence Nationale de la Recherche ANR-20 CE12-0025Agence Nationale de la Recherche ANR-21-CE20-0003Agence Nationale de la Recherche ANR-25-CE20-0508
6 · The paper itself

Abstract

Cytoplasmic biomolecular condensates are membrane-less structures important for cell homeostasis, especially during stress conditions. These aggregates concentrate RNA, protein, and metabolites during a wide variety of stresses. The formation of cytoplasmic biomolecular condensates was studied extensively in plants, revealing many key actors involved in their nucleation. More recently, post-translational modifications (PTMs) of some of these components appear as a novel layer in cytoplasmic biomolecular condensate formation. Here, we describe the importance of the PTMs in cytoplasmic biomolecular condensate dynamics in plants. We highlight the major contribution of phosphorylation and ubiquitination in these processes and discuss the involvement of other recently discovered PTMs.

Indexed as

Biomolecular CondensatesCytoplasmPlantsProtein Processing, Post-TranslationalPhosphorylationPlant ProteinsUbiquitinationPlant Proteinscytoplasmic biomolecular condensatesgranulesliquid–liquid phase separationpost‐translational modificationsstress

Identifiers

PMID40999735
PMCPMC12529029

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.