Peptide affinity purification for the isolation and identification of GPCR-associated protein complexes.
Methods Mol Biol
; 746: 389-98, 2011.
Article
en En
| MEDLINE
| ID: mdl-21607870
ABSTRACT
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Proteínas Portadoras
/
Cromatografía de Afinidad
/
Receptores Acoplados a Proteínas G
/
Complejos Multiproteicos
Tipo de estudio:
Diagnostic_studies
/
Risk_factors_studies
Límite:
Animals
Idioma:
En
Revista:
Methods Mol Biol
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2011
Tipo del documento:
Article
País de afiliación:
Francia