Molecular Mechanisms of Go Signaling
Open Access
- 1 January 2009
- journal article
- review article
- Published by S. Karger AG in Neurosignals
- Vol. 17 (1), 23-41
- https://doi.org/10.1159/000186688
Abstract
Go is the most abundant G protein in the central nervous system, where it comprises about 1% of membrane protein in mammalian brains. It functions to couple cell surface receptors to intercellular effectors, which is a critical process for cells to receive, interpret and respond to extracellular signals. Go protein belongs to the pertussis toxin-sensitive Gi/Go subfamily of G proteins. A number of G-protein-coupled receptors transmit stimuli to intercellular effectors through Go. Go regulates several cellular effectors, including ion channels, enzymes, and even small GTPases to modulate cellular function. This review summarizes some of the advances in Go research and proposes areas to be further addressed in exploring the functional role of Go.Keywords
This publication has 96 references indexed in Scilit:
- Activation of the cloned muscarinic potassium channel by G protein βγ subunitsNature, 1994
- Reduced concentrations of the ?-subunit of GTP-binding protein Go in schizophrenic brainJournal of Neural Transmission, 1994
- G proteins (Gi, Go) in the medial temporal lobe in schizophrenia: preliminary report of a neurochemical correlate of structural changeJournal of Neural Transmission, 1991
- G-proteins (Gi, Go) in the basal ganglia of control and schizophrenic brainJournal of Neural Transmission, 1990
- Molecular cloning and sequence determination of four different cDNA species coding for α‐subunits of G proteins from Xenopus laevis oocytesFEBS Letters, 1990
- Neuroblastoma Differentiation Involves the Expression of Two Isoforms of the α‐Subunit of GoJournal of Neurochemistry, 1990
- Purification of GTP‐binding proteins from bovine brain membranesFEBS Letters, 1989
- Identification of both Gi2 and a novel, immunologically distinct, form of Go in rat myometrial membranesFEBS Letters, 1989
- Presence of three pertussis toxin substrates and Goα immunoreactivity in both plasma and granule membranes of chromaffin cellsFEBS Letters, 1987
- Changes in axonally transported proteins during axon regeneration in toad retinal ganglion cells.The Journal of cell biology, 1981