Evidence map›Paper›PMID 30962358›Full record

ArticleMolecular systems biology2019

The fitness cost and benefit of phase-separated protein deposits.

Natalia Sanchez de Groot, Marc Torrent Burgas, Charles Nj Ravarani, Ala Trusina, Salvador Ventura, M Madan Babu

Open access · goldAbstract read
In one paragraph

Article in Molecular systems biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

8 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Development of a Positive Selection High Throughput Genetic Screen inFrontiers in cell and developmental biology · 2021
    Article
  5. Article
  6. Article
  7. Using protein engineering to understand and modulate aggregation.Current opinion in structural biology · 2020
    Review
  8. 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

6 authors at 3 institutions in 3 countries.

Natalia Sanchez de GrootMedical Research Council Laboratory of Molecular Biology, Cambridge, UK natalia.sanchez@crg.eu madanm@mrc-lmb.cam.ac.uk.ORCID 0000-0002-0492-5532
Marc Torrent BurgasMedical Research Council Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0001-6567-3474
Charles Nj RavaraniMedical Research Council Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0003-0952-3396
Ala TrusinaNiels Bohr Institute, University of Copenhagen, Copenhagen, Denmark.
Salvador VenturaInstitut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Barcelona, Spain.ORCID 0000-0002-9652-6351
M Madan BabuMedical Research Council Laboratory of Molecular Biology, Cambridge, UK natalia.sanchez@crg.eu madanm@mrc-lmb.cam.ac.uk.ORCID 0000-0003-0556-6196
MRC Laboratory of Molecular Biology · GBUniversitat Autònoma de Barcelona · ESUniversity of Copenhagen · DK

Funding

Medical Research Council MC_U105185859
6 · The paper itself

Abstract

Phase separation of soluble proteins into insoluble deposits is associated with numerous diseases. However, protein deposits can also function as membrane-less compartments for many cellular processes. What are the fitness costs and benefits of forming such deposits in different conditions? Using a model protein that phase-separates into deposits, we distinguish and quantify the fitness contribution due to the loss or gain of protein function and deposit formation in yeast. The environmental condition and the cellular demand for the protein function emerge as key determinants of fitness. Protein deposit formation can influence cell-to-cell variation in free protein abundance between individuals of a cell population (i.e., gene expression noise). This results in variable manifestation of protein function and a continuous range of phenotypes in a cell population, favoring survival of some individuals in certain environments. Thus, protein deposit formation by phase separation might be a mechanism to sense protein concentration in cells and to generate phenotypic variability. The selectable phenotypic variability, previously described for prions, could be a general property of proteins that can form phase-separated assemblies and may influence cell fitness.

Indexed as

Fungal ProteinsGenetic FitnessSaccharomyces cerevisiaeSelection, GeneticSystems BiologyFungal Proteinscell fitnessnatural selectionphase separationphenotypic diversityprotein deposit

Identifiers

PMID30962358
PMCPMC6452874
OpenAlexW2952973455

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.