G protein-coupled receptor interacting proteins: emerging roles in localization and signal transduction

Cell Signal. 2002 Apr;14(4):297-309. doi: 10.1016/s0898-6568(01)00239-x.


The mechanism by which G protein-coupled receptors (GPCRs) translate extracellular signals into cellular changes initially was envisioned as a simple linear model: activation of the receptor by agonist binding leads to dissociation of the heterotrimeric GTP-binding G protein into its alpha and betagamma subunits, both of which can activate or inhibit various downstream effector molecules. The plethora of recently described multidomain scaffolding proteins and accessory/chaperone molecules that interact with GPCR, including GPCR themselves as homo- or heterodimers, provides for diverse molecular mechanisms for ligand recognition, signalling specificity, and receptor trafficking. This review will summarize the recently described GPCR-interacting proteins and their individual functional roles, as understood. Implicit in the search for the functional relevance of these interactions is the expectation that enhancement or disruption of target cell-specific events could serve as highly selective therapeutic opportunities.

Publication types

  • Review

MeSH terms

  • Cell Membrane / metabolism
  • Dimerization
  • Heterotrimeric GTP-Binding Proteins / metabolism*
  • Macromolecular Substances
  • Molecular Chaperones / metabolism
  • Protein Structure, Tertiary
  • Receptors, Cell Surface / metabolism
  • Signal Transduction*


  • Macromolecular Substances
  • Molecular Chaperones
  • Receptors, Cell Surface
  • Heterotrimeric GTP-Binding Proteins