The C-Terminal Domains of the GABABReceptor Subunits Mediate Intracellular Trafficking But Are Not Required for Receptor Signaling

• DOI: 10.1523/jneurosci.21-04-01203.2001
• Publication Date: 2018-04-05T00:12:27Z
• Authors: Andrew R. Calver; Melanie J. Robbins; Christophe Cosio; Simon Q. J. Rice; Adam J. Babbs; Warren D. Hirst; Izzy Boyfield; Martyn D. Wood; Robert B. Russell; Gary W. Price; Andrés Couve; Stephen J. Moss; Menelas N. Pangalos
• Keywords: Homomeric; Gamma-Aminobutyric Acid

GABA B receptors are G-protein-coupled that mediate slow synaptic inhibition in the brain and spinal cord. These heterodimers assembled from B1 B2 subunits, neither of which is capable producing functional on homomeric expression. B1, although able to bind GABA, retained within endoplasmic reticulum (ER) when expressed alone. In contrast, access cell surface alone but does not couple efficiently appropriate effector systems or produce any detectable GABA-binding sites. present study, we have constructed chimeric truncated subunits explore further receptor signaling assembly. Removal entire C-terminal intracellular domain results plasma membrane expression without production a receptor. However, coexpression this subunit with either C terminal has also been removed via G-proteins. transferring tail leads ER retention indicate mediates protein tails an absolute requirement for coupling heteromeric receptors. Furthermore sites, central importance G-proteins subsequent activation systems.