期刊
EMBO JOURNAL
卷 30, 期 18, 页码 3842-3853出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/emboj.2011.276
关键词
gephyrin; GlyR beta-loop; ITC; PKC; SPT
资金
- INSERM
- Institut pour la Recherche sur la Moelle Epiniere et l'Encephale (IRME)
- Fondation Pierre-Gilles de Gennes
- German Science Foundation (DFG) [Schw 759/8-1]
- CMMC
Glycine receptors (GlyRs) can dynamically exchange between synaptic and extrasynaptic locations through lateral diffusion within the plasma membrane. Their accumulation at inhibitory synapses depends on the interaction of the beta-subunit of the GlyR with the synaptic scaffold protein gephyrin. An alteration of receptor-gephyrin binding could thus shift the equilibrium between synaptic and extrasynaptic GlyRs and modulate the strength of inhibitory neurotransmission. Using a combination of dynamic imaging and biochemical approaches, we have characterised the molecular mechanism that links the GlyR-gephyrin interaction with GlyR diffusion and synaptic localisation. We have identified a protein kinase C (PKC) phosphorylation site within the cytoplasmic domain of the beta-subunit of the GlyR (residue S403) that causes a reduction of the binding affinity between the receptor and gephyrin. In consequence, the receptor's diffusion in the plasma membrane is accelerated and GlyRs accumulate less strongly at synapses. We propose that the regulation of GlyR dynamics by PKC thus contributes to the plasticity of inhibitory synapses and may be involved in maladaptive forms of synaptic plasticity. The EMBO Journal (2011) 30, 3842-3853. doi: 10.1038/emboj.2011.276; Published online 9 August 2011
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据