Ligand-triggered de-repression of Arabidopsis heterotrimeric G proteins coupled to immune receptor kinases View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-05

AUTHORS

Xiangxiu Liang, Miaomiao Ma, Zhaoyang Zhou, Jinlong Wang, Xinru Yang, Shaofei Rao, Guozhi Bi, Lin Li, Xiaojuan Zhang, Jijie Chai, She Chen, Jian-Min Zhou

ABSTRACT

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. More... »

PAGES

529-543

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41422-018-0027-5

DOI

http://dx.doi.org/10.1038/s41422-018-0027-5

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1101543406

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29545645


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