ArticleThe Journal of biological chemistry2012
The intrinsically disordered N-terminal region of AtREM1.3 remorin protein mediates protein-protein interactions.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 75 citations in OpenAlex.
- Functional Genomics Screening inEnvironmental science & technology · 2026Article
- Membrane nanodomains to shape plant cellular functions and signaling.The New phytologist · 2025Review
- Dynamic pre-structuration of lipid nanodomain-segregating remorin proteins.Communications biology · 2024Article
- XopM, An FFAT Motif-Containing Type III Effector Protein From Xanthomonas, Suppresses MTI Responses at the Plant Plasma Membrane.Molecular plant pathology · 2024Article
- Genome-Wide Identification of theLife (Basel, Switzerland) · 2024Article
- Stress-induced nuclear translocation of ONAC023 improves drought and heat tolerance through multiple processes in rice.Nature communications · 2024Article
- The type III effector NopL interacts with GmREM1a and GmNFR5 to promote symbiosis in soybean.Nature communications · 2024Article
- Genome-wide characterization of Remorin gene family and their responsive expression to abiotic stresses and plant hormone in Brassica napus.Plant cell reports · 2024Article
- Identification and characterization of theFrontiers in plant science · 2024Article
- Characterization of Intrinsically Disordered Proteins in Healthy and Diseased States by Nuclear Magnetic Resonance.Reviews on recent clinical trials · 2024Review
- Structural determinants of REMORIN nanodomain formation in anionic membranes.Biophysical journal · 2023Article
- Mutations in CmVPS41 controlling resistance to cucumber mosaic virus display specific subcellular localization.Plant physiology · 2023Article
- Stabilization of membrane topologies by proteinaceous remorin scaffolds.Nature communications · 2023Article
- Candidate pathogenicity factor/effector proteins of 'Frontiers in plant science · 2023Article
- Palmitoylation Is Indispensable for Remorin to Restrict Tobacco Mosaic Virus Cell-to-Cell Movement inViruses · 2022Article
- Membrane nanodomains modulate formin condensation for actin remodeling in Arabidopsis innate immune responses.The Plant cell · 2022Article
- Connecting the dots: from nanodomains to physiological functions of REMORINs.Plant physiology · 2021Review
- Interesting Biochemistries in the Structure and Function of Bacterial Effectors.Frontiers in cellular and infection microbiology · 2021Review
- The Nanoscale Organization of the Plasma Membrane and Its Importance in Signaling: A Proteolipid Perspective.Plant physiology · 2020Review
- Deviating from the Beaten Track: New Twists in Brassinosteroid Receptor Function.International journal of molecular sciences · 2020Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The longstanding structure-function paradigm, which states that a protein only serves a biological function in a structured state, had to be substantially revised with the description of intrinsic disorder in proteins. Intrinsically disordered regions that undergo a stimulus-dependent disorder-to-order transition are common to a large number of signaling proteins. However, little is known about the functionality of intrinsically disordered regions in plant proteins. Here we investigated intrinsic disorder in a plant-specific remorin protein that has been described as a signaling component in plant-microbe interactions. Using bioinformatic, biochemical, and biophysical approaches, we characterized the highly abundant remorin AtREM1.3, showing that its N-terminal region is intrinsically disordered. Although only the AtREM1.3 C-terminal domain is essential for stable homo-oligomerization, the N-terminal region facilitates this interaction. Furthermore, we confirmed the stable interaction between AtREM1.3 and four isoforms of the importin α protein family in a yeast two-hybrid system and by an in planta bimolecular fluorescent complementation assay. Phosphorylation of Ser-66 in the intrinsically disordered N-terminal region decreases the interaction strength with the importin α proteins. Hence, the N-terminal region may constitute a regulatory domain, stabilizing these interactions.
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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 OpenQuestion graph.