Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 371652
Title Fluorescence fluctuation analysis of Arabidopsis thaliana somatic embryogenesis receptor-like kinase and brassinosteriod insensitive 1 receptor oligomerization
Author(s) Hink, M.A.; Shah, K.; Russinova, E.T.; Vries, S.C. de; Visser, A.J.W.G.
Source Biophysical Journal 94 (2008). - ISSN 0006-3495 - p. 1052 - 1062.
DOI https://doi.org/10.1529/biophysj.107.112003
Department(s) Biochemistry
EPS-1
Publication type Refereed Article in a scientific journal
Publication year 2008
Keyword(s) cross-correlation spectroscopy - protein-protein interactions - photon-counting histogram - live cells - signal-transduction - imaging microscopy - fusion proteins - plasma-membrane - energy-transfer - living cells
Abstract Receptor kinases play a key role in the cellular perception of signals. To verify models for receptor activation through dimerization, an experimental system is required to determine the precise oligomerization status of proteins within living cells. Here we show that photon counting histogram analysis and dual-color fluorescence cross correlation spectroscopy are able to monitor fluorescently labeled proteins at the single-molecule detection level in living plant cells. In-frame fusion proteins of the brassinosteroid insensitive 1 (BRI1) receptor and the Arabidopsis thaliana somatic embryogenesis receptor-like kinases 1 and 3 (AtSERK1 and 3) to the enhanced cyan or yellow fluorescent protein were transiently expressed in plant cells. Although no oligomeric structures were detected for AtSERK3, 15% (AtSERK1) to 20% (BRI1) of the labeled proteins in the plasma membrane was found to be present as homodimers, whereas no evidence was found for higher oligomeric complexes.
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