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

Copyright © 2015 Elsevier GmbH. All rights reserved.

Détails bibliographiques
Publié dans:Journal of plant physiology. - 1979. - 188(2015) vom: 01. Sept., Seite 44-8
Auteur principal: Aranda-Sicilia, María Nieves (Auteur)
Autres auteurs: Trusov, Yuri, Maruta, Natsumi, Chakravorty, David, Zhang, Yuelin, Botella, José Ramón
Format: Article en ligne
Langue:English
Publié: 2015
Accès à la collection:Journal of plant physiology
Sujets:Journal Article Research Support, Non-U.S. Gov't Arabidopsis Heterotrimeric G proteins Plant defence Protein–protein interaction Receptor-like kinases (RLKs) Arabidopsis Proteins Protein Serine-Threonine Kinases EC 2.7.11.1 plus... Heterotrimeric GTP-Binding Proteins EC 3.6.5.1
Description
Résumé:Copyright © 2015 Elsevier GmbH. All rights reserved.
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
Description:Date Completed 08.08.2016
Date Revised 03.12.2021
published: Print-Electronic
Citation Status MEDLINE
ISSN:1618-1328
DOI:10.1016/j.jplph.2015.09.005