| First Author | Yang J | Year | 2011 |
| Journal | EMBO J | Volume | 30 |
| Issue | 1 | Pages | 165-80 |
| PubMed ID | 21119615 | Mgi Jnum | J:168713 |
| Mgi Id | MGI:4936793 | Doi | 10.1038/emboj.2010.286 |
| Citation | Yang J, et al. (2011) DGKiota regulates presynaptic release during mGluR-dependent LTD. EMBO J 30(1):165-80 |
| abstractText | 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 DGKiota. In addition, we establish that DGKiota acts presynaptically, a function that contrasts with the known postsynaptic function of DGKzeta, a close relative of DGKiota. Deficiency of DGKiota in mice does not affect dendritic spines, but leads to a small increase in presynaptic release probability. In addition, DGKiota-/- synapses show a reduction in metabotropic glutamate receptor-dependent long-term depression (mGluR-LTD) at neonatal ( approximately 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 DGKiota-/- synapses. These results suggest that DGKiota requires PSD-95 family proteins for synaptic localization and regulates presynaptic DAG signalling and neurotransmitter release during mGluR-LTD. |
