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Jan 2011 Methods in molecular biology (Clifton, N.J.)

Peptide affinity purification for the isolation and identification of GPCR-associated protein complexes.

Auteurs

Maurice P, Daulat AM, Jockers R

Résumé

Protein networks and their dynamic regulation play a fundamental role in biological systems. Seven transmembrane-spanning G protein-coupled receptors (GPCRs) constitute the largest family of membrane receptors controlling the flow of information from the extracellular environment into cells by inducing intracellular signaling pathways. Several GPCR-associated protein complexes (GAPCs), particularly those binding to the intracellular carboxyl-terminus (C-terminus), have been identified over the last 20 years. Recent optimizations in purification protocols and advances in mass spectrometry-based protein identification techniques have considerably accelerated the identification of GAPCs. We will concentrate here on a description of the latest version of the peptide affinity purification approach dedicated to the purification of GAPCs interacting with GPCR C-termini or any other soluble receptor subdomain.

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