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PMID: 18552232 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Interactions between the S-domain receptor kinases and AtPUB-ARM E3 ubiquitin ligases suggest a conserved signaling pathway in Arabidopsis.

Plant physiology ·Vol. 147 ·No. 4 ·2008-08-00 ·Pages 2084-95

Samuel MA, Mudgil Y, Salt JN, Delmas F, Ramachandran S, Chilelli A, Goring DR

Abstract

The Arabidopsis (Arabidopsis thaliana) genome encompasses multiple receptor kinase families with highly variable extracellular domains. Despite their large numbers, the various ligands and the downstream interacting partners for these kinases have been deciphered only for a few members. One such member, the S-receptor kinase, is known to mediate the self-incompatibility (SI) response in Brassica. S-receptor kinase has been shown to interact and phosphorylate a U-box/ARM-repeat-containing E3 ligase, ARC1, which, in turn, acts as a positive regulator of the SI response. In an effort to identify conserved signaling pathways in Arabidopsis, we performed yeast two-hybrid analyses of various S-domain receptor kinase family members with representative Arabidopsis plant U-box/ARM-repeat (AtPUB-ARM) E3 ligases. The kinase domains from S-domain receptor kinases were found to interact with ARM-repeat domains from AtPUB-ARM proteins. These kinase domains, along with M-locus protein kinase, a positive regulator of SI response, were also able to phosphorylate the ARM-repeat domains in in vitro phosphorylation assays. Subcellular localization patterns were investigated using transient expression assays in tobacco (Nicotiana tabacum) BY-2 cells and changes were detected in the presence of interacting kinases. Finally, potential links to the involvement of these interacting modules to the hormone abscisic acid (ABA) were investigated. Interestingly, AtPUB9 displayed redistribution to the plasma membrane of BY-2 cells when either treated with ABA or coexpressed with the active kinase domain of ARK1. As well, T-DNA insertion mutants for ARK1 and AtPUB9 lines were altered in their ABA sensitivity during germination and acted at or upstream of ABI3, indicating potential involvement of these proteins in ABA responses.

MeSH Terms
Abscisic Acid/pharmacology Arabidopsis/drug effects,enzymology,genetics Arabidopsis Proteins/analysis,chemistry,metabolism Cell Membrane/metabolism Cells, Cultured Germination/genetics Phosphorylation Plant Growth Regulators/pharmacology Plants, Genetically Modified/metabolism Protein Kinases/analysis,chemistry,metabolism Protein Structure, Tertiary Seeds/genetics,growth & development,metabolism Signal Transduction Tobacco/genetics Two-Hybrid System Techniques Ubiquitin-Protein Ligases/analysis,chemistry,metabolism
Chemicals
Arabidopsis Proteins Plant Growth Regulators Abscisic Acid Ubiquitin-Protein Ligases Protein Kinases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Samuel Marcus A
Department of Cell and Systems Biology, University of Toronto, Toronto, Ontario, Canada M5S 3B2.
Mudgil Yashwanti
Salt Jennifer N
Delmas Frédéric
Ramachandran Shaliny
Chilelli Andrea
Goring Daphne R
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Article Info
Journal
Plant physiology
Abbr.
Plant Physiol
ISSN
0032-0889
Published
2008-08-00
Epub
2008-00-13
Pages
2084-95
Language
English
Region
United States
NLM ID
0401224
PMCID
PMC2492606
Subset
IM
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