Evidence map›Paper›PMID 34090478›Full record

ArticleCell communication and signaling : CCS2021

Sequence determinants of in cell condensate morphology, dynamics, and oligomerization as measured by number and brightness analysis.

Ryan J Emenecker, Alex S Holehouse, Lucia C Strader

Abstract read
In one paragraph

Article in Cell communication and signaling : CCS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

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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

12 citing papers in PubMed.

  1. AUXIN RESPONSE FACTOR thermostability.Nature communications · 2026
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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

3 authors.

Ryan J EmeneckerDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, 63110, USA.
Alex S HolehouseDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, 63110, USA. alex.holehouse@wustl.edu.
Lucia C StraderCenter for Science and Engineering Living Systems (CSELS), Washington University, St. Louis, MO, 63130, USA. lucia.strader@duke.edu.ORCID 0000-0002-7600-7204

Funding

NIGMS administrative equipment supplement for R35 GM136338-02R35GM136338 · NIGMS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI Lucia Strader · 2020 to 2026
$3.2M
NIGMS NIH HHS R35 GM136338
6 · The paper itself

Abstract

backgroundBiomolecular condensates are non-stoichiometric assemblies that are characterized by their capacity to spatially concentrate biomolecules and play a key role in cellular organization. Proteins that drive the formation of biomolecular condensates frequently contain oligomerization domains and intrinsically disordered regions (IDRs), both of which can contribute multivalent interactions that drive higher-order assembly. Our understanding of the relative and temporal contribution of oligomerization domains and IDRs to the material properties of in vivo biomolecular condensates is limited. Similarly, the spatial and temporal dependence of protein oligomeric state inside condensates has been largely unexplored in vivo.

methodsIn this study, we combined quantitative microscopy with number and brightness analysis to investigate the aging, material properties, and protein oligomeric state of biomolecular condensates in vivo. Our work is focused on condensates formed by AUXIN RESPONSE FACTOR 19 (ARF19), a transcription factor integral to the auxin signaling pathway in plants. ARF19 contains a large central glutamine-rich IDR and a C-terminal Phox Bem1 (PB1) oligomerization domain and forms cytoplasmic condensates.

resultsOur results reveal that the IDR amino acid composition can influence the morphology and material properties of ARF19 condensates. In contrast the distribution of oligomeric species within condensates appears insensitive to the IDR composition. In addition, we identified a relationship between the abundance of higher- and lower-order oligomers within individual condensates and their apparent fluidity.

conclusionsIDR amino acid composition affects condensate morphology and material properties. In ARF condensates, altering the amino acid composition of the IDR did not greatly affect the oligomeric state of proteins within the condensate. Video Abstract.

Indexed as

Protein MultimerizationArabidopsisArabidopsis ProteinsBiomolecular CondensatesFluorescenceIntrinsically Disordered ProteinsMembrane FluidityTranscription FactorsArabidopsis ProteinsARF19 protein, ArabidopsisIntrinsically Disordered ProteinsTranscription FactorsBiomolecular condensatesFluorescence microscopyFluorescence recovery after photobleachingIntrinsically disordered regionsNumber and brightness analysis

Identifiers

PMID34090478
PMCPMC8178893

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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.