title: Non-canonical signaling and localizations of heterotrimeric G proteins.
abstract: Heterotrimeric G proteins typically transduce signals from G protein-coupled receptors (GPCRs) to effector proteins. In the conventional G protein signaling paradigm, the G protein is located at the cytoplasmic surface of the plasma membrane, where, after activation by an agonist-bound GPCR, the GTP-bound Gα and free Gβγ bind to and regulate a number of well-studied effectors, including adenylyl cyclase, phospholipase Cβ, RhoGEFs and ion channels. However, research over the past decade or more has established that G proteins serve non-canonical roles in the cell, whereby they regulate novel effectors, undergo activation independently of a GPCR, and/or function at subcellular locations other than the plasma membrane. This review will highlight some of these non-canonical aspects of G protein signaling, focusing on direct interactions of G protein subunits with cytoskeletal and cell adhesion proteins, the role of G proteins in cell division, and G protein signaling at diverse organelles.
authors: Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, United States.
authors: Thamara
authors: T
authors: Hewavitharana
authors: Philip B
authors: PB
authors: Wedegaertner
mesh_terms: D000818:Animals; D015815:Cell Adhesion Molecules / Q000378:metabolism; D002455:Cell Division; D003598:Cytoskeletal Proteins / Q000378:metabolism; D020962:Heterotrimeric GTP-Binding Proteins / Q000378:metabolism*; D006801:Humans; D015388:Organelles / Q000378:metabolism; D011485:Protein Binding; D021381:Protein Transport; D015398:Signal Transduction
chemical_list: D015815:Cell Adhesion Molecules; D003598:Cytoskeletal Proteins; D020962:Heterotrimeric GTP-Binding Proteins