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Phosphorylation and ubiquitination of immune sensory complexes in innate immune signaling

先天免疫信号中免疫感觉复合物的磷酸化和泛素化

基本信息

批准号：
10065506
负责人：
Libo Shan
金额：
$ 26.71万
依托单位：
TEXAS A&M AGRILIFE RESEARCH
依托单位国家：
美国
项目类别：
财政年份：
2011
资助国家：
美国
起止时间：
2011-07-01 至 2022-11-30
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/10065506
关键词：
Amino Acids Animals Arabidopsis Architecture Attenuated BAK1 gene Biochemical Biological Process Biological Response Modifiers Cell Surface Receptors Cell membrane Cell physiology Cells Communicable Diseases Complex Data Detection Diacylglycerol Kinase Eukaryota Event Exposure to Flagellin Foundations Gene Expression Generations Genetic Genomics Goals Heterodimerization Immune Immune signaling Immune system Immunity Infection Knock-out Ligands Light MAP Kinase Modules Mediating Microbe Mission Modeling Molecular Monoubiquitination Natural Immunity Orthologous Gene Pattern Pattern recognition receptor Peptides Perception Phosphatidic Acid Phosphorylation Phosphotransferases Physiological Processes Plants Polyubiquitination Production Reactive Oxygen Species Receptor Signaling Regulation Research Resources Sensory Signal Transduction Structure System Testing Toll-like receptors Transgenic Organisms Ubiquitination United States National Institutes of Health antimicrobial base dimer extracellular signal-regulated kinase 4 gene function microbial microorganism novel pathogen pattern perception prevent receptor trafficking ubiquitin-protein ligase

项目摘要

Phosphorylation and ubiquitination of immune sensory complexes in innate immune signaling Project Summary Plants and animals rely on pattern-recognition receptors (PRRs) to detect infection by recognizing microbe-associated molecular patterns (MAMPs). FLS2, a structural and functional ortholog of mammalian Toll-like receptors (TLRs) in plants, recognizes bacterial flagellin and initiates immune signaling by dimerizing with a co-receptor BAK1. With the previous NIH support, we have identified a plasma membrane-tethered receptor-like cytoplasmic kinase (RLCK) BIK1 as a convergent immune regulator by association with multiple PRR complexes. MAMP perception induces rapid BIK1 phosphorylation by BAK1, and subsequent release from PRR complexes to transduce diverse immune signaling. It remains unknown how PRR-associated BIK1 is activated and then bifurcates intracellular PRR signaling. Our preliminary data indicate that MAMP perception triggers rapid mono-ubiquitination of BIK1 and related RLCKs. A RING-type E3 ubiquitin ligase BMU1, that is phosphorylated by BIK1, mediates MAMP-induced BIK1 ubiquitination. BIK1 interacts and phosphorylates a diacylglycerol kinase DGK5 that regulates MAMP-induced phosphatidic acid (PA) production. Three over-arching aims are proposed to test a central hypothesis that mono-ubiquitination of BIK1 by BMU1 triggers release of BIK1 from PRR complexes, and subsequent endosomal trafficking and relaying intracellular signaling events, including activation of DGK5 for PA production. Three specific aims are 1. Ubiquitination of BIK1 by BIK1-phosphorylated BMU1 in plant immunity; 2. Ligand-induced BIK1 mono-ubiquitination in endosomal trafficking and plant immunity; 3. Dual phosphorylation of DGK5 by PRR-activated BIK1 and MAP kinase 4 in plant immunity. Recent advance on the molecular architecture of nonself recognition has revealed remarkable conservation in the mechanisms of microbial perception and innate immune signaling in multicellular eukaryotes. Phosphorylation and ubiquitination are two key mechanisms in regulating diverse cellular and organismal processes. Our project on pathogen- induced sequential and intertwined phosphorylation and ubiquitination orchestrating PRR complex activation and signal transduction in plant immunity will generate conceptual advance in understanding the biological functions of these two universal regulatory mechanisms at the whole organismal level. The proposed research will also contribute to the general understanding of innate immune signaling and immune sensory complex function.

先天免疫信号中免疫感觉复合物的磷酸化和泛素化