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Fluorescent labeling of NK2 receptor at specific sites in vivo and fluorescence energy transfer analysis of NK2 ligand-receptor complexes

Related publications (40)

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Covalent labeling of cell-surface proteins for in-vivo FRET studies

Horst Vogel, Kai Johnsson, Rudolf Hovius, Jean-Manuel Segura, Nathalie George, Pedro Pascoal, Bruno Meyer

Fluorescence resonance energy transfer (FRET) is a powerful technique to reveal interactions between membrane proteins in live cells. Fluorescence labeling for FRET is typically performed by fusion with fluorescent proteins (FP) with the drawbacks of a lim ...

2006

Visualizing odorant receptor trafficking in living cells down to the single-molecule level

Horst Vogel, Horst Pick, Jean-Manuel Segura, Valérie Jacquier

Despite the importance of trafficking for regulating G protein-coupled receptor signaling, for many members of the seven transmembrane helix protein family, such as odorant receptors, little is known about this process in live cells. Here, the complete lif ...

2006

Investigation of the neurokinin-1 receptor by fluorescence techniques

Bruno Meyer

G protein-coupled receptors (GPCR) constitute by far the largest family of transmembrane cell-surface proteins involved in signal transduction and are the most important targets for the development of novel therapeutic compounds. Many processes mediated by ...

EPFL2005

G Protein coupled receptors (GPCRs) constitute an abundant family of membrane proteins which play a central role in cellular signaling and are important targets for modern medicine. Despite intensive research, central questions of the molecular mechanism o ...

EPFL2005

In vivo protein labeling for structural and functional investigation of the 5-HT3A neurotransmitter receptor

Erwin Ilegems

In this thesis, two different fluorescent labeling techniques for in vivo investigations on the 5-HT3 receptor (5-HT3R) functions are presented. This plasma membrane protein contains five subunits surrounding an ion channel that opens after binding of a 5- ...

EPFL2004

Reversible site-selective labeling of membrane proteins in live cells

Horst Vogel, Rudolf Hovius, Emmanuel Guignet

Chem. and biol. labeling is fundamental for the elucidation of the function of proteins within biochem. cellular networks. In particular, fluorescent probes allow detection of mol. interactions, mobility and conformational changes of proteins in live cells ...

2004

Noninvasive imaging of 5-HT3 receptor trafficking in live cells: From biosynthesis to endocytosis

Horst Vogel, Horst Pick, Cédric Deluz, Erwin Ilegems

Sequential stages in the life cycle of the ionotropic 5-HT3 receptor (5-HT3R) were resolved temporally and spatially in live cells by multicolor fluorescence confocal microscopy. The insertion of the enhanced cyan fluorescent protein into the large intrace ...

2004

Native membranes on subwavelentgh holes for membrane receptors analysis

Jürgen Brugger, Benjamin André René Meyer

How membrane receptors transduce external signals across the membrane and activate intracellular processes is a key question for fundamental research and for therapeutic purposes. Reliable in situ investigations requiest to preserve the full biological act ...

2004

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The site-specific incorporation of non-natural amino acids into proteins by nonsense suppression has been widely used to investigate protein structure and function. Usually this technique exhibits low incorporation efficiencies of non-natural amino acids i ...

2004

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Ligand-gated ion channels of the Cys loop family are receptors for small amine-contg. neurotransmitters. Charged amino acids are strongly conserved in the ligand-binding domain of these receptor proteins. To investigate the role of particular residues in l ...

2003