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Specific oligomerization of the 5-HT1A receptor in the plasma membrane

Item Type:Article
Title:Specific oligomerization of the 5-HT1A receptor in the plasma membrane
Creators Name:Woehler, A. and Wlodarczyk, J. and Ponimaskin, E.G.
Abstract:In the present study we analyze the oligomerization of the 5-HT1A receptor within living cells at the sub-cellular level. Using a 2-excitation Foerster Resonance Energy Transfer (FRET) method combined with spectral microscopy we are able to estimate the efficiency of energy transfer based on donor quenching as well as acceptor sensitization between CFP-and YFP-tagged 5-HT1A receptors at the plasma membrane. Through the analysis of the level of apparent FRET efficiency over the various relative amounts of donor and acceptor, as well as over a range of total surface expressions of the receptor, we verify the specific interaction of these receptors. Furthermore we study the role of acylation in this interaction through measurements of a palmitoylation-deficient 5-HT(1A) receptor mutant. Palmitoylation increases the tendency of a receptor to localize in lipid rich microdomains of the plasma membrane. This increases the effective surface density of the receptor and provides for a higher level of stochastic interaction.
Keywords:Palmitoylation, Serotonin, 5-HT1A receptor, Lipid rafts, FRET, Oligomerization, Animals, Mice
Source:Glycoconjugate Journal
Page Range:749-756
Date:August 2009
Official Publication:https://doi.org/10.1007/s10719-008-9187-8
PubMed:View item in PubMed

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