Stimulation- and palmitoylation-dependent changes in oligomeric conformation of serotonin 5-HT1A receptors

2008 | journal article. A publication with affiliation to the University of Göttingen.

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​Stimulation- and palmitoylation-dependent changes in oligomeric conformation of serotonin 5-HT1A receptors​
Kobe, F.; Renner, U.; Woehler, A.; Wlodarczyk, J.; Papusheva, E.; Bao, G. & Zeug, A. et al.​ (2008) 
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research1783(8) pp. 1503​-1516​.​ DOI: https://doi.org/10.1016/j.bbamcr.2008.02.021 

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Authors
Kobe, Fritz; Renner, Ute; Woehler, Andrew; Wlodarczyk, Jakub; Papusheva, Ekaterina; Bao, Guobin; Zeug, Andre; Richter, Diethelm W.; Neher, Erwin ; Ponimaskin, Evgeni G.
Abstract
In the present study we analyzed the oligomerization state of the serotonin 5-HT1A receptor and studied oligomerization dynamics in living cells. We also investigated the role of receptor palmitoylation in this process. Biochemical analysis performed in neuroblastoma N1E-115 cells demonstrated that both palmitoylated and non-palmitoylated 5-HT1A receptors form homo-oligomers and that the prevalent receptor species at the plasma membrane are dimers. A combination of an acceptor-photobleaching FRET approach with fluorescence lifetime measurements verified the interaction of CFP- and YFP-labeled wild-type as well as acylation-deficient 5-HT1A receptors at the plasma membrane of living cells. Using a novel FRET technique based on the spectral analysis we also confirmed the specific nature of receptor oligomerization. The analysis of oligomerization dynamics revealed that apparent FRET efficiency measured for wild-type oligomers significantly decreased in response to agonist stimulation, and our combined results suggest that this decrease was mediated by accumulation of FRET-negative complexes rather than by dissociation of oligomers to monomers. In contrast, the agonist-mediated decrease of FRET signal was completely abolished in oligomers composed by non-palmitoylated receptor mutants, demonstrating the importance of palmitoylation in modulation of the structure of oligomers. (C) 2008 Elsevier B.V. All rights reserved.
Issue Date
2008
Status
published
Publisher
Elsevier Science Bv
Journal
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 
ISSN
0167-4889

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