Evidence map›Paper›PMID 39843538›Full record

ArticleCommunications biology2025

Illuminating understudied kinases: a generalizable biosensor development method applied to protein kinase N.

Julius Bogomolovas, Ju Chen

Abstract read
In one paragraph

Article in Communications biology, 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. A Constellation of Fluorescent Biosensors to Illuminate the Galaxy of Protein Kinases.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Review
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

2 authors.

Julius BogomolovasDepartment of Medicine, UCSD, La Jolla, CA, USA.ORCID http://orcid.org/0000-0001-8344-1909
Ju ChenDepartment of Medicine, UCSD, La Jolla, CA, USA. juchen@ucsd.edu.ORCID http://orcid.org/0000-0001-7674-4776

Funding

U of Calif, San Diego Neuroscience Microscopy ImagingP30NS047101 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GLEESON, JOSEPH G, ZHENG, BINHAI · 2003 to 2022
$9.0M
Protein Kinase Novel 2 (PKN2) in heartR01HL155826 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHEN, JU · 2021 to 2024
$2.2M
Novel function of a mitochondria phosphatase in cardiac developmentR01HL157119 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHEN, JU · 2021 to 2024
$2.2M
ATF4 a Novel Regulator of Cardiac DevelopmentR01HL164549 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Ju Chen · 2023 to 2026
$2.2M
Nuclear envelope protein LEMD2 in heartR01HL158981 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHEN, JU · 2021 to 2024
$2.2M
Gene Therapy for ALPK3 Cardiomyopathy Using MiniALPK3R01HL175344 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Ju Chen · 2024 to 2026
$1.6M
NHLBI NIH HHS R01 HL155826NHLBI NIH HHS R01 HL157119NHLBI NIH HHS R01 HL158981NHLBI NIH HHS R01 HL164549NHLBI NIH HHS R01 HL175344NINDS NIH HHS P30 NS047101U.S. Department of Health & Human Services | NIH | National Heart, Lung, and Blood Institute (NHLBI) R01HL155826U.S. Department of Health & Human Services | NIH | National Institute of Neurological Disorders and Stroke (NINDS) P30NS047101
6 · The paper itself

Abstract

Protein kinases play crucial roles in regulating cellular processes, making real-time visualization of their activity essential for understanding signaling dynamics. While genetically encoded fluorescent biosensors have emerged as powerful tools for studying kinase activity, their development for many kinases remains challenging due to the lack of suitable substrate peptides. Here, we present a novel approach for identifying peptide substrates and demonstrate its effectiveness by developing a biosensor for Protein Kinase N (PKN) activity. Our method identified a new PKN substrate peptide that we optimized for use in a fluorescent biosensor design. The resulting biosensor shows specificity for PKN family kinases and can detect both overexpressed and endogenous PKN activity in live cells. Importantly, our biosensor revealed sustained basal PKN2 activity at the plasma membrane, identifying it as a PKN2 activity hotspot. This work not only provides a valuable tool for studying PKN signaling but also demonstrates a promising strategy for developing biosensors for other understudied kinases, potentially expanding our ability to monitor kinase activity across the human kinome.

Indexed as

Biosensing TechniquesProtein Kinase CHEK293 CellsHumansPeptidesPhosphorylationSignal TransductionSubstrate SpecificityPeptidesProtein Kinase Cprotein kinase N

Identifiers

PMID39843538
PMCPMC11754634

What Socratic 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 Socratic graph.