A proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptorsReport as inadecuate




A proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptors - Download this document for free, or read online. Document in PDF available to download.

Biological Procedures Online

, Volume 4, Issue 1, pp 94–104

Received: 17 September 2002Revised: 14 November 2002Accepted: 15 November 2002DOI: 10.1251-bpo39

Cite this article as: Bécamel, C., Galéotti, N., Poncet, J. et al. Biol Proced Online 2002 4: 94. doi:10.1251-bpo39

Abstract

There is accumulating evidence that membrane-bound receptors interact with many intracellular proteins. Multiprotein complexes associated with ionotropic receptors have been extensively characterized, but the identification of proteins interacting with G protein-coupled receptors GPCRs has so far only been achieved in a piecemeal fashion, focusing on one or two protein species. We describe a method based on peptide affinity chromatography, two-dimensional electrophoresis, mass spectrometry and immunoblotting to identify the components of multiprotein complexes interacting directly or indirectly with intracellular domains of GPCRs or, more generally, any other membrane-bound receptor. Using this global approach, we have characterized multiprotein complexes that bind to the carboxy-terminal tail of the 5-hydroxytryptamine type 2C receptor and are important for its subcellular localization in CNS cells Bécamel et al., EMBO J., 2110: 2332, 2002.

Indexing termsproteomics spectrum analysis, mass Published: December 9, 2002

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Author: Carine Bécamel - Nathalie Galéotti - Joël Poncet - Patrick Jouin - Aline Dumuis - Joël Bockaert - Philippe Marin

Source: https://link.springer.com/







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