Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractDeciphering the Metabolic Pathways of Pitaya Peel after Postharvest Red Light Irradiation    Next AbstractEffects of antibiotics on anaerobic digestion of sewage sludge: Performance of anaerobic digestion and structure of the microbial community »

New Phytol


Title:The carboxy-terminal tail of GLR3.3 is essential for wound-response electrical signaling
Author(s):Wu Q; Stolz S; Kumari A; Farmer EE;
Address:"Shenzhen Branch, Guangdong Laboratory of Lingnan Modern Agriculture, Genome Analysis Laboratory of the Ministry of Agriculture and Rural Affairs, Agricultural Genomics Institute at Shenzhen, Chinese Academy of Agricultural Sciences, Shenzhen, 518120, China. Department of Plant Molecular Biology, Biophore, University of Lausanne, Lausanne, CH-1015, Switzerland"
Journal Title:New Phytol
Year:2022
Volume:20220928
Issue:6
Page Number:2189 - 2201
DOI: 10.1111/nph.18475
ISSN/ISBN:1469-8137 (Electronic) 0028-646X (Print) 0028-646X (Linking)
Abstract:"Arabidopsis Clade 3 GLUTAMATE RECEPTOR-LIKEs (GLRs) are primary players in wound-induced systemic signaling. Previous studies focused on dissecting their ligand-activated channel properties involving extracellular and membrane-related domains. Here, we report that the carboxy-terminal tails (C-tails) of GLRs contain key elements controlling their function in wound signaling. GLR3.3 without its C-tail failed to rescue the glr3.3a mutant. We carried out a yeast two-hybrid screen to identify the C-tail interactors. We performed functional studies of the interactor by measuring electrical signals and defense responses. Then we mapped their binding sites and evaluated the impact of the sites on GLR functions. IMPAIRED SUCROSE INDUCTION 1 (ISI1) interacted with GLR3.3. Enhanced electrical activity was detected in reduced function isi1 mutants in a GLR3.3-dependent manner. isi1 mutants were slightly more resistant to insect feeding than the wild-type. Furthermore, a triresidue motif RFL in the GLR3.3 C-tail binds to ISI1 in yeast. Finally, we demonstrated that FL residues were conserved across GLRs and functionally required. Our study provides new insights into the functions of GLR C-tails, reveals parallels with the ionotropic glutamate receptor regulation in animal cells, and may enable rational design of strategies to engineer GLRs for future practical applications"
Keywords:"Animals *Arabidopsis Proteins/genetics/metabolism Saccharomyces cerevisiae/metabolism *Arabidopsis/metabolism Receptors, Glutamate/genetics/metabolism Signal Transduction Arabidopsis defense electrical signaling glutamate receptor herbivory jasmonate phlo;"
Notes:"MedlineWu, Qian Stolz, Stephanie Kumari, Archana Farmer, Edward E eng Research Support, Non-U.S. Gov't England 2022/09/13 New Phytol. 2022 Dec; 236(6):2189-2201. doi: 10.1111/nph.18475. Epub 2022 Sep 28"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 16-11-2024