Evidence map›Paper›PMID 36163138›Full record

ArticleNature communications2022

The material properties of a bacterial-derived biomolecular condensate tune biological function in natural and synthetic systems.

Keren Lasker, Steven Boeynaems, Vinson Lam, Daniel Scholl, Emma Stainton, Adam Briner, Maarten Jacquemyn, Dirk Daelemans, Ashok Deniz, Elizabeth Villa and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
10.2field-weighted citation impact, top 1% 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

85 citing papers in PubMed, 126 citations in OpenAlex.

  1. Article
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  8. Chemical reviews · 2026
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Sticky interactions govern sequence-dependent dynamics in biomolecular condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  14. Article
  15. Biomolecular Condensates Can Induce Local Membrane Potentials.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Accurate prediction of thermoresponsive phase behavior of disordered proteins.Protein science : a publication of the Protein Society · 2025
    Article

25 more citing papers are in PubMed but not listed here.

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

13 authors at 8 institutions in 3 countries.

Keren Lasker *Department of Developmental Biology, Stanford University School of Medicine, Stanford, CA, USA. klasker@scripps.edu.
Steven Boeynaems *Department of Genetics, Stanford University School of Medicine, Stanford, CA, USA.
Vinson LamDepartment of Molecular Biology, School of Biological Sciences, University of California San Diego, La Jolla, CA, USA.
Daniel SchollDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, USA.
Emma StaintonDepartment of Developmental Biology, Stanford University School of Medicine, Stanford, CA, USA.ORCID 0000-0002-4247-8059
Adam BrinerClem Jones Centre for Ageing Dementia Research (CJCADR), Queensland Brain Institute (QBI), The University of Queensland, Brisbane, QLD, Australia.ORCID 0000-0002-4760-5037
Maarten JacquemynKU Leuven Department of Microbiology, Immunology, and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, KU Leuven, Leuven, Belgium.ORCID 0000-0003-2626-4189
Dirk DaelemansKU Leuven Department of Microbiology, Immunology, and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, KU Leuven, Leuven, Belgium.ORCID 0000-0001-7092-1153
Ashok DenizDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, USA.
Elizabeth VillaDepartment of Molecular Biology, School of Biological Sciences, University of California San Diego, La Jolla, CA, USA.ORCID 0000-0003-4677-9809
Alex S HolehouseDepartment of Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, MO, USA.ORCID 0000-0002-4155-5729
Aaron D GitlerDepartment of Genetics, Stanford University School of Medicine, Stanford, CA, USA. agitler@stanford.edu.ORCID 0000-0001-8603-1526
Lucy ShapiroDepartment of Developmental Biology, Stanford University School of Medicine, Stanford, CA, USA. shapiro@stanford.edu.ORCID 0000-0002-0445-067X
Scripps Research Institute · USRega Institute for Medical Research · BEStanford Medicine · USStanford University · USHoward Hughes Medical Institute · USThe University of Queensland · AUUniversity of California San Diego · USWashington University in St. Louis · US

Funding

Innovating Yeast and Human Genetics Approaches to Define Mechanisms of Neurodegenerative DiseaseR35NS097263 · NINDS · STANFORD UNIVERSITY · PI GITLER, AARON D. · 2017 to 2024
$8.6M
Undergraduate Summer Research Experience: Molecular and cellular mechanisms of circadian timekeeping in a prokaryote modelR35GM118290 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GOLDEN, SUSAN S · 2016 to 2025
$6.7M
Integration of regulatory networks and subcellular architecture to control the Caulobacter cell cycleR35GM118071 · NIGMS · STANFORD UNIVERSITY · PI SHAPIRO, LUCILLE · 2016 to 2020
$3.2M
Opening Windows into the Cell: Revealing the Molecular Architecture of the Nuclear PeripheryDP2GM123494 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI VILLA, ELIZABETH · 2016 to 2019
$2.5M
Biophysics of Protein Disorder and Complexity, Single Molecules to MesoscalesR35GM130375 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DENIZ, ASHOK A · 2019 to 2023
$2.4M
Defining modifiers and mechanisms of RAN translationR01AG064690 · NIA · STANFORD UNIVERSITY · PI Aaron D. Gitler, JOSEPH D PUGLISI · 2024 to 2026
$2.3M
Howard Hughes Medical InstituteNIA NIH HHS R01 AG064690NIGMS NIH HHS DP2 GM123494NIGMS NIH HHS R35 GM118071NIGMS NIH HHS R35 GM118290NIGMS NIH HHS R35 GM130375NINDS NIH HHS R35 NS097263
6 · The paper itself

Abstract

Intracellular phase separation is emerging as a universal principle for organizing biochemical reactions in time and space. It remains incompletely resolved how biological function is encoded in these assemblies and whether this depends on their material state. The conserved intrinsically disordered protein PopZ forms condensates at the poles of the bacterium Caulobacter crescentus, which in turn orchestrate cell-cycle regulating signaling cascades. Here we show that the material properties of these condensates are determined by a balance between attractive and repulsive forces mediated by a helical oligomerization domain and an expanded disordered region, respectively. A series of PopZ mutants disrupting this balance results in condensates that span the material properties spectrum, from liquid to solid. A narrow range of condensate material properties supports proper cell division, linking emergent properties to organismal fitness. We use these insights to repurpose PopZ as a modular platform for generating tunable synthetic condensates in human cells.

Indexed as

Caulobacter crescentusIntrinsically Disordered ProteinsBacterial ProteinsBiomolecular CondensatesCell DivisionHumansBacterial ProteinsIntrinsically Disordered Proteins

Identifiers

PMID36163138
PMCPMC9512792
OpenAlexW4297222089

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.