ArticleeLife2025
Interdependence of plasma membrane nanoscale dynamics of a kinase and its cognate substrate underlies
Article in eLife, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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.
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Who cites it
7 citing papers in PubMed.
- Mechanisms controlling the plasma membrane targeting and the nanodomain organization of the plant SPFH protein HIR2.The Plant journal : for cell and molecular biology · 2026Article
- The diverse roles of host membranes in plant-microbe interactions.PLoS pathogens · 2026Article
- Interdependence of plasma membrane nanoscale dynamics of a kinase and its cognate substrate underlieseLife · 2025Article
- Membrane nanodomains to shape plant cellular functions and signaling.The New phytologist · 2025Review
- Arabidopsis Calcium Dependent Protein Kinase 3, and Its Orthologues OsCPK1, OsCPK15, and AcCPK16, Are Involved in Biotic and Abiotic Stresses.Plants (Basel, Switzerland) · 2025Article
- Calcium signaling: an emerging player in plant antiviral defense.Journal of experimental botany · 2024Article
- OneFlowTraX: a user-friendly software for super-resolution analysis of single-molecule dynamics and nanoscale organization.Frontiers in plant science · 2024Article
Corrections and comments
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Authors and funding
22 authors.
Funding
Abstract
Plant viruses represent a risk to agricultural production and as only a few treatments exist, it is urgent to identify resistance mechanisms and factors. In plant immunity, plasma membrane (PM)-localized proteins play an essential role in sensing the extracellular threat presented by bacteria, fungi, or herbivores. Viruses are intracellular pathogens and as such the role of the plant PM in detection and resistance against viruses is often overlooked. We investigated the role of the partially PM-bound Calcium-dependent protein kinase 3 (CPK3) in viral infection and we discovered that it displayed a specific ability to hamper viral propagation over CPK isoforms that are involved in immune response to extracellular pathogens. More and more evidence supports that the lateral organization of PM proteins and lipids underlies signal transduction in plants. We showed here that CPK3 diffusion in the PM is reduced upon activation as well as upon viral infection and that such immobilization depended on its substrate, Remorin (REM1.2), a scaffold protein. Furthermore, we discovered that the viral infection induced a CPK3-dependent increase of REM1.2 PM diffusion. Such interdependence was also observable regarding viral propagation. This study unveils a complex relationship between a kinase and its substrate that contrasts with the commonly described co-stabilisation upon activation while it proposes a PM-based mechanism involved in decreased sensitivity to viral infection in plants.
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Identifiers
What Socratic holds
Registered trials
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.