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异源三聚体G蛋白在拟南芥中与防御相关的类受体激酶相互作用。

Heterotrimeric G proteins interact with defense-related receptor-like kinases in Arabidopsis.

作者信息

Aranda-Sicilia María Nieves, Trusov Yuri, Maruta Natsumi, Chakravorty David, Zhang Yuelin, Botella José Ramón

机构信息

School of Agriculture and Food Sciences, University of Queensland, Brisbane, QLD 4072, Australia; Current address: Department of Plant Biochemistry, Molecular and Cell Biology, Estación Experimental del Zaidín, CSIC, 18008 Granada, Spain.

School of Agriculture and Food Sciences, University of Queensland, Brisbane, QLD 4072, Australia.

出版信息

J Plant Physiol. 2015 Sep 1;188:44-8. doi: 10.1016/j.jplph.2015.09.005. Epub 2015 Sep 24.

Abstract

Heterotrimeric G proteins (G-proteins) are versatile signaling elements conserved in Eukaryotes. In animals G-proteins relay signals from 7-transmembrane spanning G protein-coupled receptors (GPCRs) to intracellular downstream effectors; however, the existence of GPCRs in plants is controversial. Contrastingly, a surplus of receptor-like kinases (RLKs) provides signal recognition at the plant cell surface. It is established that G proteins are involved in plant defense and suggested that they relay signals from defense-related RLKs. However, it is unclear how the signaling is conducted, as physical interaction between the RLKs and G proteins has not been demonstrated. Using yeast split-ubiquitin system and Bimolecular Fluorescence Complementation assays, we demonstrate physical interaction between the Gα, Gγ1 and Gγ2 subunits, and the defense-related RD-type receptor like kinases CERK1, BAK1 and BIR1. At the same time, no interaction was detected with the non-RD RLK FLS2. We hypothesize that G-proteins mediate signal transduction immediately downstream of the pathogenesis-related RLKs.

摘要

异源三聚体G蛋白(G蛋白)是真核生物中保守的多功能信号元件。在动物中,G蛋白将信号从7次跨膜的G蛋白偶联受体(GPCR)传递到细胞内下游效应器;然而,植物中GPCR的存在存在争议。相比之下,大量的类受体激酶(RLK)在植物细胞表面提供信号识别。已经确定G蛋白参与植物防御,并表明它们传递来自与防御相关的RLK的信号。然而,由于尚未证明RLK与G蛋白之间的物理相互作用,信号传导是如何进行的尚不清楚。使用酵母分裂泛素系统和双分子荧光互补分析,我们证明了Gα、Gγ1和Gγ2亚基与防御相关的RD型类受体激酶CERK1、BAK1和BIR1之间的物理相互作用。同时,未检测到与非RD RLK FLS2的相互作用。我们假设G蛋白在与发病机制相关的RLK的紧邻下游介导信号转导。

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