Evidence map›Paper›PMID 35171683›Full record

ArticleScience advances2022

ATP-responsive biomolecular condensates tune bacterial kinase signaling.

Saumya Saurabh, Trisha N Chong, Camille Bayas, Peter D Dahlberg, Heather N Cartwright, W E Moerner, Lucy Shapiro

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.2field-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

44 citing papers in PubMed, 74 citations in OpenAlex.

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  14. Interfacial effects determine nonequilibrium phase behaviors in chemically driven fluids.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
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  17. Adaptive ATP-induced molecular condensation in membranized protocells.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Article
  19. In situ architecture of a nucleoid-associated biomolecular co-condensate that regulates bacterial cell division.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  20. 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

7 authors at 2 institutions in 1 country.

Saumya SaurabhDepartment of Developmental Biology, Stanford University School of Medicine, Stanford, CA, USA.ORCID 0000-0002-7524-7548
Trisha N ChongDepartment of Developmental Biology, Stanford University School of Medicine, Stanford, CA, USA.ORCID 0000-0002-0888-8441
Camille BayasDepartment of Chemistry, Stanford University, Stanford, CA, USA.
Peter D DahlbergDepartment of Chemistry, Stanford University, Stanford, CA, USA.ORCID 0000-0003-4452-2663
Heather N CartwrightDepartment of Plant Biology, Carnegie Institution for Science, Stanford, CA, USA.
W E MoernerDepartment of Chemistry, Stanford University, Stanford, CA, USA.ORCID 0000-0002-2830-209X
Lucy ShapiroDepartment of Developmental Biology, Stanford University School of Medicine, Stanford, CA, USA.ORCID 0000-0002-0445-067X
Stanford University · USCarnegie Institution for Science · US

Funding

Single-Molecule Imaging for Cell Biology and Super-Resolution MicroscopyR35GM118067 · NIGMS · STANFORD UNIVERSITY · PI MOERNER, WILLIAM E · 2016 to 2025
$6.2M
Integration of regulatory networks and subcellular architecture to control the Caulobacter cell cycleR35GM118071 · NIGMS · STANFORD UNIVERSITY · PI SHAPIRO, LUCILLE · 2016 to 2020
$3.2M
NIGMS NIH HHS R35 GM118067NIGMS NIH HHS R35 GM118071
6 · The paper itself

Abstract

Biomolecular condensates formed via liquid-liquid phase separation enable spatial and temporal organization of enzyme activity. Phase separation in many eukaryotic condensates has been shown to be responsive to intracellular adenosine triphosphate (ATP) levels, although the consequences of these mechanisms for enzymes sequestered within the condensates are unknown. Here, we show that ATP depletion promotes phase separation in bacterial condensates composed of intrinsically disordered proteins. Enhanced phase separation promotes the sequestration and activity of a client kinase enabling robust signaling and maintenance of viability under the stress posed by nutrient scarcity. We propose that a diverse repertoire of condensates can serve as control knobs to tune enzyme sequestration and reactivity in response to the metabolic state of bacterial cells.

Indexed as

Adenosine TriphosphateIntrinsically Disordered ProteinsAdenosine KinaseBacteriaBiomolecular CondensatesHumansAdenosine KinaseAdenosine TriphosphateIntrinsically Disordered Proteins

Identifiers

PMID35171683
PMCPMC8849385
OpenAlexW4220839844

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.