ArticlePlant physiology2012
Plasma membrane localization of Solanum tuberosum remorin from group 1, homolog 3 is mediated by conformational changes in a novel C-terminal anchor and required for the restriction of potato virus X movement].
Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 98 citations in OpenAlex.
- The Arabidopsis SPFH protein HIR2 modulates receptor signaling and plasma membrane organization.The EMBO journal · 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
- Revealing plasma membrane protein dynamics in living plant cells with single-molecule tracking.Journal of experimental botany · 2025Article
- 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
- CDPK5 and CDPK13 play key roles in acclimation to low oxygen through the control of RBOH-mediated ROS production in rice.Plant physiology · 2024Article
- Dynamic pre-structuration of lipid nanodomain-segregating remorin proteins.Communications biology · 2024Article
- A viral protein activates the MAPK pathway to promote viral infection by downregulating callose deposition in plants.Nature communications · 2024Article
- Genome-Wide Identification of theLife (Basel, Switzerland) · 2024Article
- Guidelines for naming and studying plasma membrane domains in plants.Nature plants · 2024Review
- RinRK1 enhances NF receptors accumulation in nanodomain-like structures at root-hair tip.Nature communications · 2024Article
- Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins.International journal of molecular sciences · 2024Review
- Identification and characterization of theFrontiers in plant science · 2024Article
- Structural determinants of REMORIN nanodomain formation in anionic membranes.Biophysical journal · 2023Article
- Hello darkness, my old friend: 3-KETOACYL-COENZYME A SYNTHASE4 is a branch point in the regulation of triacylglycerol synthesis in Arabidopsis thaliana.The Plant cell · 2023Article
- CaREM1.4 interacts with CaRIN4 to regulateHorticulture research · 2023Article
- Stabilization of membrane topologies by proteinaceous remorin scaffolds.Nature communications · 2023Article
- Molecular characterization and expression analysis of theFrontiers in plant science · 2023Article
- Tackling functional redundancy of Arabidopsis fatty acid elongase complexes.Frontiers in plant science · 2023Article
- Palmitoylation Is Indispensable for Remorin to Restrict Tobacco Mosaic Virus Cell-to-Cell Movement inViruses · 2022Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formation of plasma membrane (PM) microdomains plays a crucial role in the regulation of membrane signaling and trafficking. Remorins are a plant-specific family of proteins organized in six phylogenetic groups, and Remorins of group 1 are among the few plant proteins known to specifically associate with membrane rafts. As such, they are valuable to understand the molecular bases for PM lateral organization in plants. However, little is known about the structural determinants underlying the specific association of group 1 Remorins with membrane rafts. We used a structure-function approach to identify a short C-terminal anchor (RemCA) indispensable and sufficient for tight direct binding of potato (Solanum tuberosum) REMORIN 1.3 (StREM1.3) to the PM. RemCA switches from unordered to α-helical structure in a nonpolar environment. Protein structure modeling indicates that RemCA folds into a tight hairpin of amphipathic helices. Consistently, mutations reducing RemCA amphipathy abolished StREM1.3 PM localization. Furthermore, RemCA directly binds to biological membranes in vitro, shows higher affinity for Detergent-Insoluble Membranes lipids, and targets yellow fluorescent protein to Detergent-Insoluble Membranes in vivo. Mutations in RemCA resulting in cytoplasmic StREM1.3 localization abolish StREM1.3 function in restricting potato virus X movement. The mechanisms described here provide new insights on the control and function of lateral segregation of plant PM.
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