title: G protein trafficking.
abstract: The classical view of heterotrimeric G protein signaling places G -proteins at the cytoplasmic surface of the cell's plasma membrane where they are activated by an appropriate G protein-coupled receptor. Once activated, the GTP-bound Gα and the free Gβγ are able to regulate plasma membrane-localized effectors, such as adenylyl cyclase, phospholipase C-β, RhoGEFs and ion channels. Hydrolysis of GTP by the Gα subunit returns the G protein to the inactive Gαβγ heterotrimer. Although all of these events in the G protein cycle can be restricted to the cytoplasmic surface of the plasma membrane, G protein localization is dynamic. Thus, it has become increasingly clear that G proteins are able to move to diverse subcellular locations where they perform non-canonical signaling functions. This chapter will highlight our current understanding of trafficking pathways that target newly synthesized G proteins to the plasma membrane, activation-induced and reversible translocation of G proteins from the plasma membrane to intracellular locations, and constitutive trafficking of G proteins.
authors.affiliation: Department of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 S. 10th St., 839 BLSB, Philadelphia, PA, 19107-5541, USA, philip.wedegaertner@jefferson.edu.
authors.forename: Philip B
authors.initials: PB
authors.lastname: Wedegaertner
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006801:Humans; D021381:Protein Transport; D043562:Receptors, G-Protein-Coupled / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: D043562:Receptors, G-Protein-Coupled