The plant immune receptor FLS2 regulates the G protein activation pattern through RGS1.

The heterogenous tripolymer G protein is widely present in eukaryotic cells and plays an important regulatory role in cell life activity.
in animal cells, G-protein alpha sub-receptor (G protein-coupled receptor, GPCR) binding, GPCR receptor, play the role of bird nucleotide exchange factor, promote G alpha sub-binding GDP is replaced by GTP, resulting in G protein activation, G alpha sub-cells and G beta dipolymer dilated, activated G protein through the downstream target transmission and amplification.
rgS protein with GTP hydrolysis accelerated activity (GTPase accelerated protein, GAP) by enhancing the hydrolysis enzyme activity of G alpha, enabling GTP to be rapidly hydrolyzed to GDP and the G protein to return to resting state.
different from animal cells, there is no GPCR protein in plant cells, and plant G alpha protein has the self-activation ability of active binding GTP, so how plant cells regulate G protein activation has been a major problem in the field of plant science research.
the amoeba immune receptor FLS2 can sense the invasion of pathogenic bacteria by identifying bacterial whiplash proteins, and activate the downstream immune response through the core kinase BIK1 of the immune receptor complex.
an earlier study by Zhou Jianmin of the Institute of Genetics and Developmental Biology of the Chinese Academy of Sciences found that G protein plays an important regulatory role in the immune response mediated by FLS2.
heterogenous triples consisting of G-alpha proteins (XLG2 and XLG3), G-beta proteins (AGB1) and G-gamma proteins (AGG1 and AGG2) are directly tripled with FLS2.
but the molecular mechanism of how immune receptor FLS2 regulates G protein activation is not clear.
In the latest study, the Genetic Development Institute's Zhou Jianmin research team revealed the molecular mechanism of the amoeba immune receptor FLS2 regulating plant G protein activation.
in a state of rest, the only RGS protein RGS1 of the amoeba is combined with g alpha protein and immune receptor FLS2, and the GTP binding to G alpha protein is hydrolyzed to GDP through the GAP activity of RGS1, thus maintaining the G protein in a resting state.
after the sensation of whiplash protein in FLS2, BIK1 phosphorylation RGS1 proteinSer431 and Ser428, resulting in the dissocing of RGS1 with G alpha sub-and FLS2, de-irisation of RGS1 on G-alpha, G-alpha was activated by automatic allying GTP and promoting immune response.
, XLG2 regulates the immune response in leaf cells, while GPA1 prevents the invasion of pathogenic microorganisms by regulating the closure of the pores.
the new activation of the animal G protein, which is different from the plant cell G protein, is achieved by receptor-induced the phosphorylation of RGS1, thus de-inhibiting G alpha.
related research results published in Cell Research, post-doctoral Liang Xiangxiu, Ph.D. student Ma Miao miao as the paper co-first author.
the research was funded by the National Natural Science Foundation of China, the Ministry of Science and Technology, the Chinese Academy of Sciences strategic pilot science and technology special and plant genomics national key laboratory.
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