title: Fluorescence fluctuation analysis of receptor kinase dimerization.
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.
authors.affiliation: Department of Molecular Cytology, van Leeuwenhoek Centre for Advanced Microscopy (LCAM), University of Amsterdam, Amsterdam, The Netherlands. m.a.hink@uva.nl
authors.forename: Mark A
authors.initials: MA
authors.lastname: Hink
authors.forename: Sacco C
authors.initials: SC
authors.lastname: de Vries
authors.forename: Antonie J W G
authors.initials: AJ
authors.lastname: Visser
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D002138:Calibration; D005470:Fluorometry / Q000379:methods*; D018506:Gene Expression Regulation, Plant; D005822:Genetic Vectors / Q000235:genetics; D011494:Protein Kinases / Q000235:genetics / Q000378:metabolism*; D055503:Protein Multimerization; D011523:Protoplasts / Q000378:metabolism; D013050:Spectrometry, Fluorescence / Q000379:methods; D014162:Transfection
chemical_list: D029681:Arabidopsis Proteins; D011494:Protein Kinases; C440035:SERK1 protein, Arabidopsis