TY - JOUR KW - Science & Technology KW - Life Sciences & Biomedicine KW - Cell Biology KW - GABA(B) RECEPTOR INTERNALIZATION KW - GAMMA-AMINOBUTYRIC-ACID KW - CENTRAL-NERVOUS-SYSTEM KW - PROTEIN-KINASE KW - LATERAL MOBILITY KW - INHIBITORY NEUROTRANSMISSION KW - HETEROSYNAPTIC DEPRESSION KW - SURFACE TRAFFICKING KW - SYNAPTIC PLASTICITY KW - SUSHI DOMAINS; AMPK; bungarotoxin binding site; Ca2+ signaling; excitotoxicity; GABA receptors; GABAB receptors; glutamate receptors; hippocampus; homeostatic signaling; lateral diffusion; NMDA receptors; phosphorylation; presynaptic terminal; quantum dots; receptor mobility; single-particle tracking; sushi domains ID - discovery1508144 N2 - Here, we uncover a mechanism for regulating the number of active presynaptic GABAB receptors (GABABRs) at nerve terminals, an important determinant of neurotransmitter release. We find that GABABRs gain access to axon terminals by lateral diffusion in the membrane. Their relative accumulation is dependent upon agonist activation and the presence of the two distinct sushi domains that are found only in alternatively spliced GABABR1a subunits. Following brief activation of NMDA receptors (NMDARs) using glutamate, GABABR diffusion is reduced, causing accumulation at presynaptic terminals in a Ca2+-dependent manner that involves phosphorylation of GABABR2 subunits at Ser783. This signaling cascade indicates how synaptically released glutamate can initiate, via a feedback mechanism, increased levels of presynaptic GABABRs that limit further glutamate release and excitotoxicity. PB - CELL PRESS TI - Phospho-dependent Accumulation of GABABRs at Presynaptic Terminals after NMDAR Activation EP - 1973 AV - public Y1 - 2016/08/16/ JF - Cell Reports A1 - Hannan, S A1 - Gerrow, K A1 - Triller, A A1 - Smart, TG SN - 2211-1247 UR - http://doi.org/10.1016/j.celrep.2016.07.021 N1 - © 2016 The Author(s). This is an open access article under the Creative Commons Attribution 4.0 International (CC BY 4.0) license (http://creativecommons.org/licenses/by/4.0/) IS - 7 VL - 16 SP - 1962 ER -