A proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptors |
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Authors: | Carine Bécamel Nathalie Galéotti Joël Poncet Patrick Jouin Aline Dumuis Joël Bockaert Philippe Marin |
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Institution: | (1) CNRS UPR 9023, 141, Rue de la Cardonille, 34094 Montpellier Cedex 5, France |
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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., 21(10): 2332, 2002).
Published: December 9, 2002 |
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Keywords: | Indexing terms" target="_blank">Indexing terms proteomics spectrum analysis mass |
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