Arabidopsis heterotrimeric G proteins regulate diverse processes by coupling to single-transmembrane receptors. One such receptor is the FLS2 receptor kinase, which perceives bacterial flagellin epitope flg22 to activate immunity through a class of cytoplasmic kinases called BIK1/PBLs. Unlike animal and fungal heterotrimeric G proteins that are activated by a ligand-induced guanine nucleotide exchange activity of seven-transmembrane G protein-coupled receptors (GPCRs), plant heterotrimeric G proteins are self-activating. How plant receptors regulate heterotrimeric G proteins in response to external ligands remains unknown. Here we show that RGS1, a GTPase accelerating protein, maintains Arabidopsis G proteins in an inactive state in complex with FLS2. Activation of FLS2 by flg22 induces a BIK1/PBL-mediated phosphorylation of RGS1 at Ser428 and Ser431 and that promotes RGS1 dissociation from the FLS2-G protein complex. This relieves G proteins from the RGS1-mediated repression and enables positive regulation of immune signaling. We additionally show that RGS1 is similarly regulated by multiple immune receptors. Our results uncover ligand-induced de-repression as a mechanism for G protein signaling in plants that is distinct from previously reported mechanism underlying the activation of heterotrimeric G proteins in other systems.
Ligand-triggered de-repression of Arabidopsis heterotrimeric G proteins coupled to immune receptor kinases
Xiangxiu Liang,Miaomiao Ma,Zhaoyang Zhou,Jinlong Wang,Xinru Yang,Shaofei Rao,Guozhi Bi,Lin Li,Xiaojuan Zhang,J. Chai,She Chen,Jian‐Min Zhou
Published 2018 in Cell Research
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- Publication year
2018
- Venue
Cell Research
- Publication date
2018-03-15
- Fields of study
Biology, Medicine, Environmental Science
- Identifiers
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- Source metadata
Semantic Scholar, PubMed
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