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GTP-Binding Protein alpha Subunits
About: GTP-Binding Protein alpha Subunits is a research topic. Over the lifetime, 304 publications have been published within this topic receiving 19915 citations.
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TL;DR: This review focuses on the coupling specificity of the Galpha and Gbetagamma subunits of pertussis toxin-sensitive G(i/o) proteins that mediate diverse signaling pathways, including regulation of ion channels and other effectors.
173 citations
TL;DR: The first 15 years or so brought the realization that there existed a G protein coupled signal transduction mechanism by which hormone receptors regulate adenylyl cyclases and the light receptor rhodopsin activates visual phosphodiesterase as discussed by the authors.
152 citations
TL;DR: It is demonstrated that G(alpha)(i) is not only a donor of G(beta)(gamma) but also regulates GIRK gating, and is regulated, in distinct ways, by both arms of the G protein.
152 citations
TL;DR: Cryo-electron microscopy structures of human neurotensin receptor 1 in complex with Gi1 protein and the agonist JMV449 reveal a non-canonical state that may represent an intermediate form in G-protein activation.
Abstract: Neurotensin receptor 1 (NTSR1) is a G-protein-coupled receptor (GPCR) that engages multiple subtypes of G protein, and is involved in the regulation of blood pressure, body temperature, weight and the response to pain. Here we present structures of human NTSR1 in complex with the agonist JMV449 and the heterotrimeric Gi1 protein, at a resolution of 3 A. We identify two conformations: a canonical-state complex that is similar to recently reported GPCR–Gi/o complexes (in which the nucleotide-binding pocket adopts more flexible conformations that may facilitate nucleotide exchange), and a non-canonical state in which the G protein is rotated by about 45 degrees relative to the receptor and exhibits a more rigid nucleotide-binding pocket. In the non-canonical state, NTSR1 exhibits features of both active and inactive conformations, which suggests that the structure may represent an intermediate form along the activation pathway of G proteins. This structural information, complemented by molecular dynamics simulations and functional studies, provides insights into the complex process of G-protein activation. Cryo-electron microscopy structures of human neurotensin receptor 1 in complex with Gi1 protein and the agonist JMV449 reveal a non-canonical state that may represent an intermediate form in G-protein activation.
152 citations
TL;DR: The discovery of subtype-selective mechanisms of G protein activation illustrates that G protein subfamilies have specific mechanisms of activation that may provide a previously unknown basis for G protein signaling specificity.
152 citations