ArticlePloS one2012
Functional domain analysis of the Remorin protein LjSYMREM1 in Lotus japonicus.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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48 citing papers in PubMed, 103 citations in OpenAlex.
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- The type III effector NopL interacts with GmREM1a and GmNFR5 to promote symbiosis in soybean.Nature communications · 2024Article
- RinRK1 enhances NF receptors accumulation in nanodomain-like structures at root-hair tip.Nature communications · 2024Article
- Identification and characterization of theFrontiers in plant science · 2024Article
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- Stabilization of membrane topologies by proteinaceous remorin scaffolds.Nature communications · 2023Article
- Molecular characterization and expression analysis of theFrontiers in plant science · 2023Article
- Detection of candidate gene networks involved in resistance to Sclerotinia sclerotiorum in soybean.Journal of applied genetics · 2022Review
- Plasma membrane nano-organization specifies phosphoinositide effects on Rho-GTPases and actin dynamics in tobacco pollen tubes.The Plant cell · 2021Article
- Connecting the dots: from nanodomains to physiological functions of REMORINs.Plant physiology · 2021Review
- Remorins: Essential Regulators in Plant-Microbe Interaction and Cell Death Induction.Plant physiology · 2020Article
- TheThe Plant cell · 2020Article
- The Nanoscale Organization of the Plasma Membrane and Its Importance in Signaling: A Proteolipid Perspective.Plant physiology · 2020Review
- Receptor-Like Kinases Sustain Symbiotic Scrutiny.Plant physiology · 2020Review
- Legume genomics and transcriptomics: From classic breeding to modern technologies.Saudi journal of biological sciences · 2020Review
- Organization and dynamics of functional plant membrane microdomains.Cellular and molecular life sciences : CMLS · 2020Review
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In legumes rhizobial infection during root nodule symbiosis (RNS) is controlled by a conserved set of receptor proteins and downstream components. MtSYMREM1, a protein of the Remorin family in Medicago truncatula, was shown to interact with at least three receptor-like kinases (RLKs) that are essential for RNS. Remorins are comprised of a conserved C-terminal domain and a variable N-terminal region that defines the six different Remorin groups. While both N- and C-terminal regions of Remorins belonging to the same phylogenetic group are similar to each other throughout the plant kingdom, the N-terminal domains of legume-specific group 2 Remorins show exceptional high degrees of sequence divergence suggesting evolutionary specialization of this protein within this clade. We therefore identified and characterized the MtSYMREM1 ortholog from Lotus japonicus (LjSYMREM1), a model legume that forms determinate root nodules. Here, we resolved its spatio-temporal regulation and showed that over-expression of LjSYMREM1 increases nodulation on transgenic roots. Using a structure-function approach we show that protein interactions including Remorin oligomerization are mainly mediated and stabilized by the Remorin C-terminal region with its coiled-coil domain while the RLK kinase domains transiently interact in vivo and phosphorylate a residue in the N-terminal region of the LjSYMREM1 protein in vitro. These data provide novel insights into the mechanism of this putative molecular scaffold protein and underline its importance during rhizobial infection.
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