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DGKi regulates presynaptic release during mGluR-dependent LTD

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Authors
Yang, Jinhee; Seo, Jinsoo; Nair, Ramya; Han, Seungnam; Jang, Seil; Kim, Karam; Han, Kihoon; Paik, Sang Kyoo; Choi, Jeonghoon; Lee, Seunghoon; Bae, Yong Chul; Topham, Matthew K; Prescott, Stephen M; Rhee, Jeong-Seop; Choi, Se-Young; Kim, Eunjoon
Issue Date
2011-01
Publisher
Nature Publishing Group
Citation
The EMBO Journal 30:165-180
Keywords
diacylglycerol kinaselong-term depressionmetabotropic glutamate receptorsphospholipase CPSD-95
Abstract
Diacylglycerol (DAG) is an important lipid second messenger. DAG signalling is terminated by conversion of DAG to phosphatidic acid (PA) by diacylglycerol kinases (DGKs). The neuronal synapse is a major site of DAG production and action; however, how DGKs are targeted to subcellular sites of DAG generation is largely unknown. We report here that postsynaptic density (PSD)-95 family proteins interact with and promote synaptic localization of DGKl. In addition, we establish that DGKl acts presynaptically, a function that contrasts with the known postsynaptic function of DGKl, a close relative of DGKl. Deficiency of DGKl in mice does not affect dendritic spines, but leads to a small increase in presynaptic release probability. In addition, DGKl-/- synapses show a reduction in metabotropic glutamate receptor-dependent long-term depression (mGluR-LTD) at neonatal (∼2 weeks) stages that involve suppression of a decrease in presynaptic release probability. Inhibition of protein kinase C normalizes presynaptic release probability and mGluR-LTD at DGKl-/- synapses. These results suggest that DGKl requires PSD-95 family proteins for synaptic localization and regulates presynaptic DAG signalling and neurotransmitter release during mGluR-LTD.
ISSN
0261-4189
Language
English
URI
https://hdl.handle.net/10371/74187
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College of Dentistry/School of Dentistry (치과대학/치의학대학원)Dept. of Dentistry (치의학과)Journal Papers (저널논문_치의학과)
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