Publications de Erwin Ilegems | EPFL Graph Search

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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-HT3-specific neurotransmitter. The first technique, described in the first part of this report, focuses on receptor labeling via genetic fusion to spectral variants of the green fluorescent protein. I found that the resulting chimeras containing one fluore

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 intracellular loop delivered a fluorescent 5-HT3R fully functional in terms of ligand binding specificity and channel activity, which allowed for the first time a complete real-time visualization and documentation of intracellular biogenesis, membrane targeting,

Conformational changes of channel activation: Five enhanced green fluorescent protein (EGFP) mols. (green cylinders) were integrated into the intracellular part of the homopentameric ionotropic 5-HT3 receptor. This allowed the detection of extracellular bi ...

A reporter assay was developed to detect and quantify nonsense codon suppression by chem. aminoacylated tRNAs in mammalian cells. It is based on the cellular expression of the enhanced green fluorescent protein (EGFP) as a reporter for the site-specific amino acid incorporation in its sequence using an orthogonal suppressor tRNA derived from Escherichia coli. Suppression of an engineered amber codon at position 64 in the EGFP run-off transcript could be achieved by the incorporation of a leucine via an in v

Understanding cellular signaling mediated by cell surface receptors is key to modern biomedical research and drug development. The discovery of a growing no. of potential mol. targets and therapeutic compds. requires downscaling and accelerated functional ...

High signal-to-noise Fourier transform IR (FTIR) spectra of the 5-hydroxytryptamine (serotonin) receptor (5-HT3R) and the nicotinic acetylcholine receptor (nAChR) were obtained by microscope FTIR spectroscopy using micrometer-sized, fully hydrated protein films. Because this novel procedure requires only nanogram quantities of membrane proteins, which is 4-5 orders of magnitude less than the amt. of protein typically used for conventional FTIR spectroscopy, it opens the possibility to access the structure a

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 into proteins. Authors describe for the first time an approach for achieving an increased level of nonsense codon suppression with synthetic suppressor tRNAs in cultured human cells. Authors found that the intracellular concn. of the eukaryotic release fact

Erwin Ilegems

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

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

Ligand binding transmits conformational changes across the membrane-spanning region to the intracellular side of the 5-HT3 serotonin receptor

Monitoring mis-acylated tRNA suppression efficiency in mammalian cells via EGFP fluorescence recovery

Investigating cellular signaling reactions in single attoliter vesicles

Downscaling Fourier Transform Infrared Spectroscopy to the Micrometer and Nanogram Scale: Secondary Structure of Serotonin and Acetylcholine Receptors

Downregulation of eRF1 by RNA interference increases mis-acylated tRNA suppression efficiency in human cells