Fluorescence fluctuation analysis of receptor kinase dimerization.

M.A. Hink, S.C. de Vries, A.J.W.G. Visser

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

6 Citations (Scopus)

Abstract

Receptor kinases are essential for the cellular perception of signals. The classical model for activation of the receptor kinase involves dimerization, induced by the binding of the ligand. The mechanisms by which plant receptors transduce signals across the cell surface are largely unknown but plant receptors seem to dimerize as well. In this chapter, we describe two fluorescence fluctuation techniques, fluorescence cross-correlation spectroscopy and photon counting histogram analysis, to study the oligomerization state of receptor kinases in living plant cells in a quantitative manner.
Original languageEnglish
Title of host publicationMethods in Molecular Biology
Subtitle of host publicationPlant Kinases: Methods and Protocols
EditorsN. Dissmeyer, A. Schnittger
PublisherHumana Press
Pages199-215
Number of pages295
Volume779
ISBN (Electronic)9781617792649
ISBN (Print)9781617792632
DOIs
Publication statusPublished - 2011

Publication series

NameMethods in Molecular Biology
PublisherSpringer Science
Volume779
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

Keywords

  • BRI1
  • Dimerization
  • Fluorescence cross-correlation spectroscopy
  • Photon counting histogram
  • Plasma membrane
  • Protoplast
  • Receptor kinase
  • SERK1
  • SERK3

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