Journal Article

Ligand-Dependent Reduction in the Membrane Mobility of FLAGELLIN SENSITIVE2, an Arabidopsis Receptor-Like Kinase

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

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 48, issue 11, pages 1601-1611
Published in print November 2007 | ISSN: 0032-0781
Published online November 2007 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcm132
Ligand-Dependent Reduction in the Membrane Mobility of FLAGELLIN SENSITIVE2, an Arabidopsis Receptor-Like Kinase

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  • Biochemistry
  • Molecular and Cell Biology
  • Plant Sciences and Forestry

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Arabidopsis Flagellin sensitive2 (FLS2) is a transmembrane 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 μm2 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 fluorescence resonance energy transfer (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

Journal Article.  6705 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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