Mechanisms controlling the plasma membrane targeting and the nanodomain organization of the plant <scp>SPFH</scp> protein <scp>HIR2</scp>

SUMMARY Plasma membranes (PM) contain myriads of diverse nanodomains that correspond to nanometric scale structures enriched in specific lipids and proteins acting as signaling/regulation hubs involved in diverse biological processes. So far, how PM nanodomains are formed and maintained in plant cells remains largely unknown. We sought to address this question using HIR2, a plant‐specific Stomatin/Prohibitin/Flotillin/HflK/C (SPFH) domain‐containing protein that arranges in PM nanodomains, as a model. We revealed that the mono S‐acylation of Arabidopsis HIR2 either on C6 or on C7 was required for the localization of HIR2 in the PM. In addition, using state‐of‐the‐art microscopy techniques, we provided evidence that the lipid composition in sterols and very long chain fatty acids of the PM influenced HIR2 nanodomain organization. Interestingly, we highlighted that the oligomerization of HIR2 through its C‐terminal domain is essential for its organization in nanodomains and to ensure HIR2 lateral stability in the PM. HIR proteins are involved in plant immunity, and we revealed here that HIR2 nanodomain organization is required to boost the apoplastic reactive oxygen species burst induced by the bacterial peptide flg22. Overall, we propose that HIR2 nanodomain organization is a complex mechanism relying on different parameters and is essential for HIR2 function.

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Publication Details

Journal
The Plant Journal
Published
2026-05-01
DOI
https://doi.org/10.1111/tpj.70879
Primary Topic
Lipid Membrane Structure and Behavior
Type
article
Field-Weighted Citation Impact
0.00

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article

Mechanisms controlling the plasma membrane targeting and the nanodomain organization of the plant SPFH protein HIR2

Alexandre Martinière, Marcelo Nöllmann, Héla Safi, Baldwin Dumortier et al.
The Plant Journal
Lipid Membrane Structure and Behavior
article

Mechanisms controlling the plasma membrane targeting and the nanodomain organization of the plant SPFH protein HIR2

Alexandre Martinière, Marcelo Nöllmann, Héla Safi, Baldwin Dumortier, Michal Daněk, Anas Abuzeineh, Yohann Boutté, Enric Zelazny, Sébastien Mongrand, Jean-Bernard Fiche, Michaela Neubergerová, Roman Pleskot, Omar Hdedeh, Jessica Boutet, Caroline Mercier, V x E ronique Santoni, Jesús Amo, Gabriel Krouk, Amanda Martín‐Barranco
article en

Abstract

SUMMARY Plasma membranes (PM) contain myriads of diverse nanodomains that correspond to nanometric scale structures enriched in specific lipids and proteins acting as signaling/regulation hubs involved in diverse biological processes. So far, how PM nanodomains are formed and maintained in plant cells remains largely unknown. We sought to address this question using HIR2, a plant‐specific Stomatin/Prohibitin/Flotillin/HflK/C (SPFH) domain‐containing protein that arranges in PM nanodomains, as a model. We revealed that the mono S‐acylation of Arabidopsis HIR2 either on C6 or on C7 was required for the localization of HIR2 in the PM. In addition, using state‐of‐the‐art microscopy techniques, we provided evidence that the lipid composition in sterols and very long chain fatty acids of the PM influenced HIR2 nanodomain organization. Interestingly, we highlighted that the oligomerization of HIR2 through its C‐terminal domain is essential for its organization in nanodomains and to ensure HIR2 lateral stability in the PM. HIR proteins are involved in plant immunity, and we revealed here that HIR2 nanodomain organization is required to boost the apoplastic reactive oxygen species burst induced by the bacterial peptide flg22. Overall, we propose that HIR2 nanodomain organization is a complex mechanism relying on different parameters and is essential for HIR2 function.

The Plant JournalVol. 126(3)
Université Paris-Sud (FR), Centre National de la Recherche Scientifique (FR), Université de Bordeaux (FR), Inserm (FR), Université de Montpellier (FR), Charles University (CZ), Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR), Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement (FR), Centre de Biologie Structurale (FR), Institut de Biologie Intégrative de la Cellule (FR), Laboratoire de Biogenèse Membranaire (FR), CEA Paris-Saclay (FR), Institute for Neurosciences of Montpellier (FR), Institut Agro Montpelier (FR), Services déconcentrés d'appui à la recherche Occitanie-Montpellier (FR), Czech Academy of Sciences, Institute of Experimental Botany (CZ)
Agence Nationale de la Recherche, Université de Montpellier
Openalex Percentile: Top 8%
Lipid Membrane Structure and Behavior
DOISourceOpenAlex
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