ArticleThe Plant cell2022
A nanodomain-anchored scaffolding complex is required for the function and localization of phosphatidylinositol 4-kinase alpha in plants.
Article in The Plant cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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.
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.
Who cites it
18 citing papers in PubMed, 51 citations in OpenAlex.
- A STRUBBELIG-NHL3 cell surface receptor complex mediates the response to cellulose deficiency in Arabidopsis.Nature plants · 2026Article
- Phosphatidylinositol 4-phosphate; A minor lipid with multiple personalities.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2025Review
- Interdependence of plasma membrane nanoscale dynamics of a kinase and its cognate substrate underlieseLife · 2025Article
- Review
- Identity Transitions of Tapetum Phases: Insights into Vesicular Dynamics and in Mortem Support During Pollen Maturation.Plants (Basel, Switzerland) · 2025Review
- Membrane nanodomains to shape plant cellular functions and signaling.The New phytologist · 2025Review
- Identifying novel heterozygous PI4KA variants in fetal abnormalities.BMC medical genomics · 2025Article
- Genetic variations associated with adaptation in Acrocomia palms: A comparative study across the Neotropics for crop improvement.PloS one · 2025Article
- Guidelines for naming and studying plasma membrane domains in plants.Nature plants · 2024Review
- Root Walker: an automated pipeline for large scale quantification of early root growth responses at high spatial and temporal resolution.The Plant journal : for cell and molecular biology · 2024Article
- Burning questions for a warming and changing world: 15 unknowns in plant abiotic stress.The Plant cell · 2023Article
- TheeLife · 2022Article
- Phosphatidic Acid in Plant Hormonal Signaling: From Target Proteins to Membrane Conformations.International journal of molecular sciences · 2022Review
- A palmitoylation code controls PI4KIIIα complex formation and PI(4,5)P2 homeostasis at the plasma membrane.Journal of cell science · 2022Article
- Imaging the living plant cell: From probes to quantification.The Plant cell · 2022Review
- Back to the roots: A focus on plant cell biology.The Plant cell · 2022Article
- Correlative Light-Environmental Scanning Electron Microscopy of Plasma Membrane Efflux Carriers of Plant Hormone Auxin.Biomolecules · 2021Article
- Anionic phospholipid gradients: an uncharacterized frontier of the plant endomembrane network.Plant physiology · 2021Article
Corrections and comments
- Commented on by
Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphoinositides are low-abundant lipids that participate in the acquisition of membrane identity through their spatiotemporal enrichment in specific compartments. Phosphatidylinositol 4-phosphate (PI4P) accumulates at the plant plasma membrane driving its high electrostatic potential, and thereby facilitating interactions with polybasic regions of proteins. PI4Kα1 has been suggested to produce PI4P at the plasma membrane, but how it is recruited to this compartment is unknown. Here, we pin-point the mechanism that tethers Arabidopsis thaliana phosphatidylinositol 4-kinase alpha1 (PI4Kα1) to the plasma membrane via a nanodomain-anchored scaffolding complex. We established that PI4Kα1 is part of a complex composed of proteins from the NO-POLLEN-GERMINATION, EFR3-OF-PLANTS, and HYCCIN-CONTAINING families. Comprehensive knockout and knockdown strategies revealed that subunits of the PI4Kα1 complex are essential for pollen, embryonic, and post-embryonic development. We further found that the PI4Kα1 complex is immobilized in plasma membrane nanodomains. Using synthetic mis-targeting strategies, we demonstrate that a combination of lipid anchoring and scaffolding localizes PI4Kα1 to the plasma membrane, which is essential for its function. Together, this work opens perspectives on the mechanisms and function of plasma membrane nanopatterning by lipid kinases.
Indexed as
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.