Evidence map›Paper›PMID 41233332›Full record

ArticleNature communications2025

Proteomic sensors for quantitative multiplexed and spatial monitoring of kinase signaling.

William J Comstock, Marcos V A S Navarro, Deanna V Maybee, Yiseo Rho, Mateusz Wagner, Khoula Jaber, Yingzheng Wang, Marcus B Smolka

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

William J Comstock *Weill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY, USA.
Marcos V A S Navarro *Weill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY, USA.
Deanna V MaybeeWeill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY, USA.
Yiseo RhoWeill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY, USA.
Mateusz WagnerWeill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY, USA.ORCID http://orcid.org/0000-0002-4323-8516
Khoula JaberWeill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY, USA.
Yingzheng WangWeill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY, USA.
Marcus B SmolkaWeill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY, USA. mbs266@cornell.edu.ORCID http://orcid.org/0000-0001-9952-2885

Funding

Coordination of ATR Signaling for Genetic Quality Control, Silencing, and DNA Repair During MeiosisR01HD095296 · NICHD · CORNELL UNIVERSITY · PI Paula Elaine Cohen, Marcus Smolka · 2018 to 2026
$4.2M
Signaling Mechanisms in Genome Maintenance (Equipment Supplement 2023)R35GM141159 · NIGMS · CORNELL UNIVERSITY · PI Marcus Smolka · 2021 to 2026
$3.5M
Uncovering ATR signaling networks underlying chemotherapeutic synergiesF31CA281247 · NCI · CORNELL UNIVERSITY · PI COMSTOCK, WILLIAM · 2023 to 2024
$90k
NCI NIH HHS F31 CA281247NICHD NIH HHS R01 HD095296NIGMS NIH HHS R35 GM141159U.S. Department of Health & Human Services | NIH | National Cancer Institute (NCI) F31CA281247U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R01HD095296U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R35GM141159
6 · The paper itself

Abstract

Understanding kinase action requires precise quantitative measurements of their activity in vivo. In addition, the ability to capture spatial information of kinase activity is crucial to deconvolute complex signaling networks, interrogate multifaceted kinase actions, and assess drug effects or genetic perturbations. Here we develop a proteomic kinase activity sensor technique (ProKAS) for the analysis of kinase signaling using mass spectrometry. ProKAS is based on a tandem array of peptide sensors with amino acid barcodes that allow multiplexed analysis for spatial, kinetic, and screening applications. We engineered a ProKAS module to simultaneously monitor the activities of the DNA damage response kinases ATR, ATM, and CHK1 in response to genotoxic drugs, while also uncovering differences between these signaling responses in the nucleus, cytosol, and replication factories. Furthermore, we developed an in silico approach for the rational design of specific substrate peptides expandable to other kinases. Overall, ProKAS is a versatile system for systematically and spatially probing kinase action in cells.

Indexed as

Biosensing TechniquesProteomicsSignal TransductionAtaxia Telangiectasia Mutated ProteinsCheckpoint Kinase 1DNA DamageHumansMass SpectrometryPeptidesProtein KinasesAtaxia Telangiectasia Mutated ProteinsCheckpoint Kinase 1CHEK1 protein, humanPeptidesProtein Kinases

Identifiers

PMID41233332
PMCPMC12615678

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Registered trials

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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.