Evidence map›Paper›PMID 37886503›Full record

ArticlebioRxiv : the preprint server for biology2023

Direct ionic stress sensing and mitigation by the transcription factor NFAT5.

Chandni B Khandwala, Parijat Sarkar, H Broder Schmidt, Mengxiao Ma, Maia Kinnebrew, Ganesh V Pusapati, Bhaven B Patel, Desiree Tillo, Andres M Lebensohn, Rajat Rohatgi

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Chandni B KhandwalaDepartments of Biochemistry and Medicine, Stanford University School of Medicine, Stanford, CA 94305, USA.
Parijat SarkarDepartments of Biochemistry and Medicine, Stanford University School of Medicine, Stanford, CA 94305, USA.
H Broder SchmidtDepartments of Biochemistry and Medicine, Stanford University School of Medicine, Stanford, CA 94305, USA.
Mengxiao MaDepartments of Biochemistry and Medicine, Stanford University School of Medicine, Stanford, CA 94305, USA.
Maia KinnebrewDepartments of Biochemistry and Medicine, Stanford University School of Medicine, Stanford, CA 94305, USA.
Ganesh V PusapatiDepartments of Biochemistry and Medicine, Stanford University School of Medicine, Stanford, CA 94305, USA.
Bhaven B PatelDepartments of Biochemistry and Medicine, Stanford University School of Medicine, Stanford, CA 94305, USA.
Desiree TilloCenter for Cancer Research Genomics Core, National Cancer Institute, National Institutes of Health, NIH, Building 37, RM 2056B, Bethesda, MD, 20892, USA.
Andres M LebensohnLaboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, NIH, Building 37, RM 2056B, Bethesda, MD, 20892, USA.
Rajat RohatgiDepartments of Biochemistry and Medicine, Stanford University School of Medicine, Stanford, CA 94305, USA.
Stanford University · USNational Institutes of Health · US

Funding

Supplement application for an Olympus automated microscopeR35GM118082 · NIGMS · STANFORD UNIVERSITY · PI RAJAT ROHATGI · 2016 to 2026
$7.6M
NIGMS NIH HHS R35 GM118082
6 · The paper itself

Abstract

Homeostatic control of intracellular ionic strength is essential for protein, organelle and genome function, yet mechanisms that sense and enable adaptation to ionic stress remain poorly understood in animals. We find that the transcription factor NFAT5 directly senses solution ionic strength using a C-terminal intrinsically disordered region. Both in intact cells and in a purified system, NFAT5 forms dynamic, reversible biomolecular condensates in response to increasing ionic strength. This self-associative property, conserved from insects to mammals, allows NFAT5 to accumulate in the nucleus and activate genes that restore cellular ion content. Mutations that reduce condensation or those that promote aggregation both reduce NFAT5 activity, highlighting the importance of optimally tuned associative interactions. Remarkably, human NFAT5 alone is sufficient to reconstitute a mammalian transcriptional response to ionic or hypertonic stress in yeast. Thus NFAT5 is both the sensor and effector of a cell-autonomous ionic stress response pathway in animal cells.

Indexed as

biomolecular condensatescell volume regulationHOG pathwayhypertonic stressintrinsically disordered proteinion homeostasisionic strengthionic stressmacromolecular crowdingNFAT5osmolytesosmotic stressphase separationprionsTonEBPtonicitytranscription

Identifiers

PMID37886503
PMCPMC10602047
OpenAlexW4386998280

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.