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 Research, 1783(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