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Plant and Cell Physiology Advance Access originally published online on June 5, 2009
Plant and Cell Physiology 2009 50(7):1191-1200; doi:10.1093/pcp/pcp077
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© The Author 2009. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved.
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and the Japanese Society of Plant Physiologists are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

This article appears in the following Plant and Cell Physiology issue: Special Issue Articles: Omics and Bioinformatics [View the issue table of contents]

Special Issue - Regular Paper

Proteome Analysis of Detergent-Resistant Membranes (DRMs) Associated with OsRac1-Mediated Innate Immunity in Rice

Masayuki Fujiwara1,2, Satoshi Hamada2, Minori Hiratsuka2, Yoichiro Fukao1, Tsutomu Kawasaki2 and Ko Shimamoto2,*

1Laboratory of Plant Protein Analysis, Plant Education Unit, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, 630-0192 Japan
2Laboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, 630-0192 Japan

*Corresponding author: E-mail, simamoto{at}bs.naist.jp; Fax: +81-743-72-5502.


  Abstract

OsRac1, a member of the Rac/Rop GTPase family, plays important roles as a molecular switch in rice innate immunity, and the active form of OsRac1 functions in the plasma membrane (PM). To study the precise localization of OsRac1 in the PM and its possible association with other signaling components, we performed proteomic analysis of DRMs (detergent-resistant membranes) isolated from rice suspension-cultured cells transformed with myc-tagged constitutively active (CA) OsRac1. DRMs are regions of the PM that are insoluble after Triton X-100 treatment under cold conditions and are thought to be involved in various signaling processes in animal, yeast and plant cells. We identified 192 proteins in DRMs that included receptor-like kinases (RLKs) such as Xa21, nucleotide-binding leucine-rich repeat (NB-LRR)-type disease resistance proteins, a glycosylphosphatidylinositol (GPI)-anchored protein, syntaxin, NADPH oxidase, a WD-40 repeat family protein and various GTP-binding proteins. Many of these proteins have been previously identified in the DRMs isolated from other plant species, and animal and yeast cells, validating the methods used in our study. To examine the possible association of DRMs and OsRac1-mediated innate immunity, we used rice suspension-cultured cells transformed with myc-tagged wild-type (WT) OsRac1 and found that OsRac1 and RACK1A, an effector of OsRac1, shifted to the DRMs after chitin elicitor treatment. These results suggest that OsRac1-mediated innate immunity is associated with DRMs in the PM.

Keywords: Chitin elicitor - Plasma membrane - RACK1 - Rac/Rop GTPase - Rice suspension

Abbreviations: CA, constitutively active; CHAPS, 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid; DRM, detergent-resistant membrane; DTT, dithiothreitol; GPI, glycosylphosphatidylinositol; HR, hypersensitive response; IEF isoelectric focusing; LPS, lipopolysaccharide; NB-LRR, nucleotide-binding leucine-rich repeat; PAMPs, pathogen-associated molecular patterns; PBS, phosphate-buffered saline; PM, plasma membrane; PMSF, phenylmethylsulfonyl fluoride; PR, pathogenesis related; RLK, receptor-like kinase; WT, wild-type.

(Received March 31, 2009; Accepted May 29, 2009)
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