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 AbstractNew Approach of Beauveria bassiana to Control the Red Palm Weevil (Coleoptera: Curculionidae) by Trapping Technique    Next AbstractFate and transport of the beta-adrenergic agonist ractopamine hydrochloride in soil-water systems »

Plant Physiol


Title:ML3 is a NEDD8- and ubiquitin-modified protein
Author(s):Hakenjos JP; Bejai S; Ranftl Q; Behringer C; Vlot AC; Absmanner B; Hammes U; Heinzlmeir S; Kuster B; Schwechheimer C;
Address:"Department of Plant Systems Biology, Technische Universitat Munchen, 85354 Freising, Germany"
Journal Title:Plant Physiol
Year:2013
Volume:20130731
Issue:1
Page Number:135 - 149
DOI: 10.1104/pp.113.221341
ISSN/ISBN:1532-2548 (Electronic) 0032-0889 (Print) 0032-0889 (Linking)
Abstract:"NEDD8 (NEURAL PRECURSOR CELL-EXPRESSED, DEVELOPMENTALLY DOWN-REGULATED PROTEIN8) is an evolutionarily conserved 8-kD protein that is closely related to ubiquitin and that can be conjugated like ubiquitin to specific lysine residues of target proteins in eukaryotes. In contrast to ubiquitin, for which a broad range of substrate proteins are known, only a very limited number of NEDD8 target proteins have been identified to date. Best understood, and also evolutionarily conserved, is the NEDD8 modification (neddylation) of cullins, core subunits of the cullin-RING-type E3 ubiquitin ligases that promote the polyubiquitylation of degradation targets in eukaryotes. Here, we show that Myeloid differentiation factor-2-related lipid-recognition domain protein ML3 is an NEDD8- as well as ubiquitin-modified protein in Arabidopsis (Arabidopsis thaliana) and examine the functional role of ML3 in the plant cell. Our analysis indicates that ML3 resides in the vacuole as well as in endoplasmic reticulum (ER) bodies. ER bodies are Brassicales-specific ER-derived organelles and, similar to other ER body proteins, ML3 orthologs can only be identified in this order of flowering plants. ML3 gene expression is promoted by wounding as well as by the phytohormone jasmonic acid and repressed by ethylene, signals that are known to induce and repress ER body formation, respectively. Furthermore, ML3 protein abundance is dependent on NAI1, a master regulator of ER body formation in Arabidopsis. The regulation of ML3 expression and the localization of ML3 in ER bodies and the vacuole is in agreement with a demonstrated importance of ML3 in the defense to herbivore attack. Here, we extend the spectrum of ML3 biological functions by demonstrating a role in the response to microbial pathogens"
Keywords:"Amino Acid Sequence Arabidopsis/*metabolism Arabidopsis Proteins/genetics/metabolism/*physiology Endoplasmic Reticulum/metabolism Gene Expression Regulation, Plant Molecular Sequence Data Phylogeny Sequence Alignment Ubiquitination Ubiquitins/genetics/met;"
Notes:"MedlineHakenjos, Jana P Bejai, Sarosh Ranftl, Quirin Behringer, Carina Vlot, A Corina Absmanner, Birgit Hammes, Ulrich Heinzlmeir, Stephanie Kuster, Bernhard Schwechheimer, Claus eng Research Support, Non-U.S. Gov't 2013/08/02 Plant Physiol. 2013 Sep; 163(1):135-49. doi: 10.1104/pp.113.221341. Epub 2013 Jul 31"

 
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 03-07-2024