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Vol. 53, Issue 1, 1-24, March 2001
The John P. Robarts Research Institute and Departments of
Physiology, Pharmacology and Toxicology, and Medicine, University of
Western Ontario, London, Ontario, Canada
I. Introduction
II. G Protein-Coupled Receptor Desensitization
A. Protein Kinase Phosphorylation
1. Second Messenger-Dependent Protein Kinases.
2. G Protein-Coupled Receptor Kinases.
a. The G Protein-Coupled Receptor Kinase Family.
b. Targeting and Regulation.
c. Site of Action.
3. Other Kinases.
B. The Arrestins
1. The Arrestin Family.
2. Receptor Binding.
III. G Protein-Coupled Receptor Internalization
A. Molecular Mechanisms Involved in G Protein-Coupled Receptor
Endocytosis
1. Role of G Protein-Coupled Receptor Kinase and 
-Arrestin
Proteins.
2. Clathrin and -Adaptin Interactions.
3. -Arrestin Regulation.
4. Alternative G Protein-Coupled Receptor Endocytic
Pathways.
5. Receptor Determinants for Endocytosis.
B. Biological Role of G Protein-Coupled Receptor Internalization
1. Endocytosis and G Protein-Coupled Receptor
Desensitization.
2. Endocytosis and G Protein-Coupled Receptor
Resensitization.
3. Endocytosis and G Protein-Coupled Receptor
Signaling.
IV. Conclusions
Acknowledgments
References
G protein-coupled receptors (GPCRs)
are seven transmembrane proteins that form the largest single family of
integral membrane receptors. GPCRs transduce information provided by
extracellular stimuli into intracellular second messengers via their
coupling to heterotrimeric G proteins and the subsequent regulation of a diverse variety of effector systems. Agonist activation of GPCRs also
initiates processes that are involved in the feedback desensitization of GPCR responsiveness, the internalization of GPCRs, and the coupling of GPCRs to heterotrimeric G protein-independent signal transduction pathways. GPCR desensitization occurs as a consequence of
G protein uncoupling in response to phosphorylation by both second
messenger-dependent protein kinases and G protein-coupled receptor
kinases (GRKs). GRK-mediated receptor phosphorylation promotes the
binding of -arrestins, which not only uncouple receptors from
heterotrimeric G proteins but also target many GPCRs for internalization in clathrin-coated vesicles. -Arrestin-dependent endocytosis of GPCRs involves the direct interaction of the
carboxyl-terminal tail domain of -arrestins with both -adaptin
and clathrin. The focus of this review is the current and evolving
understanding of the contribution of GRKs, -arrestins, and
endocytosis to GPCR-specific patterns of desensitization and
resensitization. In addition to their role as GPCR-specific endocytic
adaptor proteins, -arrestins also serve as molecular scaffolds that
foster the formation of alternative, heterotrimeric G
protein-independent signal transduction complexes. Similar to what is
observed for GPCR desensitization and resensitization,
-arrestin-dependent GPCR internalization is involved in the
intracellular compartmentalization of these protein complexes.
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