Evidence map›Paper›PMID 39425928›Full record

ArticleCell reports2024

High-throughput identification of calcium-regulated proteins across diverse proteomes.

Timothy M Locke, Rose Fields, Hayden Gizinski, George M Otto, Melissa J S MacEwen, Domnita-Valeria Rusnac, Peixian He, David M Shechner, Chris D McGann, Matthew D Berg and 3 more

Abstract read
In one paragraph

Article in Cell reports, 2024. 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

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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Mitochondrial Calcium Signaling in Hepatocyte Health and Disease.Cold Spring Harbor perspectives in biology · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors.

Timothy M LockeDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Rose FieldsDepartment of Genome Sciences, University of Washington, Seattle, WA 98195, USA; Brotman Baty Institute for Precision Medicine, Seattle, WA, USA; Institute of Stem Cell and Regenerative Medicine, University of Washington, Seattle, WA, USA.
Hayden GizinskiDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
George M OttoDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Melissa J S MacEwenDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Domnita-Valeria RusnacDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA; Howard Hughes Medical Institute, Department of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Peixian HeDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
David M ShechnerDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Chris D McGannDepartment of Genome Sciences, University of Washington, Seattle, WA 98195, USA; Brotman Baty Institute for Precision Medicine, Seattle, WA, USA; Institute of Stem Cell and Regenerative Medicine, University of Washington, Seattle, WA, USA.
Matthew D BergDepartment of Genome Sciences, University of Washington, Seattle, WA 98195, USA.
Judit VillenDepartment of Genome Sciences, University of Washington, Seattle, WA 98195, USA.
Yasemin SancakDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA. Electronic address: sancak@uw.edu.
Devin K SchweppeDepartment of Genome Sciences, University of Washington, Seattle, WA 98195, USA; Brotman Baty Institute for Precision Medicine, Seattle, WA, USA; Institute of Stem Cell and Regenerative Medicine, University of Washington, Seattle, WA, USA. Electronic address: dkschwep@uw.edu.

Funding

Function, composition, and mechanism of RNA splicing factories in cardiomyopathyR01HL160825 · NHLBI · UNIVERSITY OF WASHINGTON · PI Charles E Murry · 2023 to 2026
$2.3M
Oligonucleotide-directed in situ proximity biotinylation: a unified method for mapping RNA-interacting proteomes, transcriptomes and genomic loci within intact cells.R01GM138799 · NIGMS · UNIVERSITY OF WASHINGTON · PI SHECHNER, DAVID MICHAEL · 2020 to 2024
$1.7M
Technology for evaluating drug-binding responses to small-molecule perturbationR35GM150919 · NIGMS · UNIVERSITY OF WASHINGTON · PI Devin Karl Schweppe · 2023 to 2026
$1.6M
The role of phosphorylation in the cellular organization of the proteomeR35GM152061 · NIGMS · UNIVERSITY OF WASHINGTON · PI Judit Villen · 2024 to 2026
$1.3M
NHLBI NIH HHS R01 HL160825NIGMS NIH HHS R01 GM138799NIGMS NIH HHS R35 GM150919NIGMS NIH HHS R35 GM152061
6 · The paper itself

Abstract

Calcium ions play important roles in nearly every biological process, yet whole-proteome analysis of calcium effectors has been hindered by a lack of high-throughput, unbiased, and quantitative methods to identify protein-calcium engagement. To address this, we adapted protein thermostability assays in budding yeast, human cells, and mouse mitochondria. Based on calcium-dependent thermostability, we identified 2,884 putative calcium-regulated proteins across human, mouse, and yeast proteomes. These data revealed calcium engagement of signaling hubs and cellular processes, including metabolic enzymes and the spliceosome. Cross-species comparison of calcium-protein engagement and mutagenesis experiments identified residue-specific cation engagement, even within well-known EF-hand domains. Additionally, we found that the dienoyl-coenzyme A (CoA) reductase DECR1 binds calcium at physiologically relevant concentrations with substrate-specific affinity, suggesting direct calcium regulation of mitochondrial fatty acid oxidation. These discovery-based proteomic analyses of calcium effectors establish a key resource to dissect cation engagement and its mechanistic effects across multiple species and diverse biological processes.

Indexed as

CalciumProteomeAnimalsHigh-Throughput Screening AssaysHumansMiceMitochondriaProteomicsSaccharomyces cerevisiaeCalciumProteomecalcium engagementcalcium ion engagementcalcium regulated proteinscell signalingCP: Cell biologyCP: Metabolismmagnesium engagementoxidation of polyunsaturated fatty acidssample multiplexed quantitationthermal stability proteomicsTMTpro

Identifiers

PMID39425928
PMCPMC11921809

What OpenQuestion holds

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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.