Skip Navigation



Plant and Cell Physiology Advance Access published online on October 9, 2007
Plant and Cell Physiology, doi:10.1093/pcp/pcm132
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow All Versions of this Article:
48/11/1601    most recent
pcm132v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Ali, u. S.
Right arrow Articles by Reddy, A.S.N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ali, u. S.
Right arrow Articles by Reddy, A.S.N.
Agricola
Right arrow Articles by Ali, u. S.
Right arrow Articles by Reddy, A.S.N.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2007. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Ligand-dependent reduction in the membrane mobility of FLAGELLIN SENSITIVE2, an Arabidopsis Receptor-like Kinase

ul Shad Ali, K.V.S.K. Prasad, Irene Day and A.S.N. Reddy*

Department of Biology and Program in Molecular Plant Biology, Colorado State University, Fort Collins, CO 80523

*Author for correspondence: A.S.N. Reddy, Department of Biology and Program in Molecular Plant Biology, Colorado State University, Fort Collins, CO 80523, Tel. 970-491-5773; Fax. 970-491-0649; E-mail. reddy{at}colostate.edu


  Abstract

Arabidopsis Flagellin sensitive2 (FLS2) is a trans-membrane leucine-rich-repeat receptor-like kinase, which recognizes a conserved 22 amino acid peptide (flg22) of bacterial flagellin and activates downstream defense signaling pathways resulting in enhanced resistance against plant pathogens. The underlying mechanisms for the activation of FLS2 in the cell membrane, however, are not fully understood. Using fluorescence recovery after photobleaching (FRAP), we demonstrate that approximately 75% of the FLS2 in the plasma membrane diffuses laterally with a diffusion coefficient of 0.34 µm s-1, indicating that it moves rapidly. Further, we show that FLS2 is less mobile in the presence of flg22 suggesting its ligand-dependent confinement to microdomains or transient interaction with other less mobile membrane proteins. Using an in vivo bimolecular fluorescence complementation (BiFC) system and FRET, which reveals in vivo protein-protein interactions, we show that FLS2 does not homodimerize either constitutively or in the presence of flg22. Our data suggest that the reduced mobility of FLS2 after binding flg22 and its existence in monomeric form are important mechanistic features of FLS2 early signaling.

Keywords: BiFC - flg22 - FRAP - FRET - membrane protein - RLK

(Received September 4, 2007; Accepted October 2, 2007)
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Plant Physiol.Home page
N. Geldner and S. Robatzek
Plant Receptors Go Endosomal: A Moving View on Signal Transduction
Plant Physiology, August 1, 2008; 147(4): 1565 - 1574.
[Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.