ArticleThe Plant cell2023
Protein S-acylation controls the subcellular localization and biological activity of PHYTOCHROME KINASE SUBSTRATE.
Article in The Plant cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Lights out: PP2C phosphatases reset phototropin signaling in darkness.The Plant cell · 2026Article
- 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
- Effector-Mediated Spatial Reprogramming of Glycolate Oxidase Subverts Peroxisomal and Membrane-Associated ROS Defences.Plant biotechnology journal · 2026Article
- Hydrogen peroxide mediates high-intensity blue light-induced hypocotyl phototropism of cotton seedlings.Stress biology · 2023Article
- Correct plasma membrane anchoring is key to PHYTOCHROME KINASE SUBSTRATE function in hypocotyl light responses.The Plant cell · 2023Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PHYTOCHROME KINASE SUBSTRATE (PKS) proteins are involved in light-modulated changes in growth orientation. They act downstream of phytochromes to control hypocotyl gravitropism in the light and act early in phototropin signaling. Despite their importance for plant development, little is known about their molecular mode of action, except that they belong to a protein complex comprising phototropins at the plasma membrane (PM). Identifying evolutionary conservation is one approach to revealing biologically important protein motifs. Here, we show that PKS sequences are restricted to seed plants and that these proteins share 6 motifs (A to F from the N to the C terminus). Motifs A and D are also present in BIG GRAIN, while the remaining 4 are specific to PKSs. We provide evidence that motif C is S-acylated on highly conserved cysteines, which mediates the association of PKS proteins with the PM. Motif C is also required for PKS4-mediated phototropism and light-regulated hypocotyl gravitropism. Finally, our data suggest that the mode of PKS4 association with the PM is important for its biological activity. Our work, therefore, identifies conserved cysteines contributing to PM association of PKS proteins and strongly suggests that this is their site of action to modulate environmentally regulated organ positioning.
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