ReviewMolecular plant-microbe interactions : MPMI2019
Regulated Disorder: Posttranslational Modifications Control the RIN4 Plant Immune Signaling Hub.
Review in Molecular plant-microbe interactions : MPMI, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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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.
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Who cites it
31 citing papers in PubMed, 74 citations in OpenAlex.
- A guardian angel: how immune factor RPS2 is activated by pathogen effector AvrRpt2.The Plant cell · 2026Article
- Cyclophilin A-mediated cis/trans isomerization modulates RIN4 to control intracellular rhizobial infection in legumes.The New phytologist · 2026Article
- Genomic Insights into Winter Wheat Breeding for Severely Cold Climates.International journal of molecular sciences · 2026Article
- Dynamic transcriptomic responses reveal candidate defense genes againstFrontiers in plant science · 2026Article
- Inhibition of rhizobial cheaters by the host Medicago truncatula involves repression of symbiotic functions and induction of defense.The New phytologist · 2025Article
- Intrinsic Disorder and Phase Separation Coordinate Exocytosis, Motility, and Chromatin Remodeling in the Human Acrosomal Proteome.Proteomes · 2025Article
- Identification of metabolic and protein markers representative of the impact of mild nitrogen deficit on agronomic performance of maize hybrids.Metabolomics : Official journal of the Metabolomic Society · 2024Article
- Stress-related transcriptomic changes associated with GFP transgene expression and active transgene silencing in plants.Scientific reports · 2024Article
- Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins.International journal of molecular sciences · 2024Review
- Subcellular spatial regulation of immunity-induced phosphorylation of RIN4 links PAMP-triggered immunity to Exo70B1.Frontiers in plant science · 2024Article
- The intrinsically disordered C-terminus of purinoceptor P2K1 fine-tunes plant responses to extracellular ATP.FEBS letters · 2023Article
- An activated form of NB-ARC protein RLS1 functions with cysteine-rich receptor-like protein RMC to trigger cell death in rice.Plant communications · 2023Article
- Deciphering the genetic architecture of resistance toFrontiers in plant science · 2023Article
- A conserved glutamate residue in RPM1-INTERACTING PROTEIN4 is ADP-ribosylated by the Pseudomonas effector AvrRpm2 to activate RPM1-mediated plant resistance.The Plant cell · 2022Article
- What's new in protein kinase/phosphatase signalling in the control of plant immunity?Essays in biochemistry · 2022Review
- Arabidopsis Plasma Membrane ATPase AHA5 Is Negatively Involved in PAMP-Triggered Immunity.International journal of molecular sciences · 2022Article
- Phosphorylation of CAD1, PLDdelta, NDT1, RPM1 Proteins Induce Resistance in Tomatoes Infected byPlants (Basel, Switzerland) · 2022Article
- Comparative and evolutionary analysis of Arabidopsis RIN4-like/NOI proteins induced by herbivory.PloS one · 2022Article
- Article
- RIN4 homologs from important crop species differentially regulate the Arabidopsis NB-LRR immune receptor, RPS2.Plant cell reports · 2021Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
Abstract
RIN4 is an intensively studied immune regulator in Arabidopsis and is involved in perception of microbial features outside and bacterial effectors inside plant cells. Furthermore, RIN4 is conserved in land plants and is targeted for posttranslational modifications by several virulence proteins from the bacterial pathogen Pseudomonas syringae. Despite the important roles of RIN4 in plant immune responses, its molecular function is not known. RIN4 is an intrinsically disordered protein (IDP), except at regions where pathogen-induced posttranslational modifications take place. IDP act as hubs for protein complex formation due to their ability to bind to multiple client proteins and, thus, are important players in signal transduction pathways. RIN4 is known to associate with multiple proteins involved in immunity, likely acting as an immune-signaling hub for the formation of distinct protein complexes. Genetically, RIN4 is a negative regulator of immunity, but diverse posttranslational modifications can either enhance its negative regulatory function or, on the contrary, render it a potent immune activator. In this review, we describe the structural domains of RIN4 proteins, their intrinsically disordered regions, posttranslational modifications, and highlight the implications that these features have on RIN4 function. In addition, we will discuss the potential role of plasma membrane subdomains in mediating RIN4 protein complex formations.
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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 OpenQuestion graph.