| First Author | Kim BY | Year | 2006 |
| Journal | Biochem Biophys Res Commun | Volume | 350 |
| Issue | 3 | Pages | 691-7 |
| PubMed ID | 17027648 | Mgi Jnum | J:263393 |
| Mgi Id | MGI:6189308 | Doi | 10.1016/j.bbrc.2006.09.104 |
| Citation | Kim BY, et al. (2006) The interaction of mammalian Class C Vps with nSec-1/Munc18-a and syntaxin 1A regulates pre-synaptic release. Biochem Biophys Res Commun 350(3):691-7 |
| abstractText | Membrane docking and fusion in neurons is a highly regulated process requiring the participation of a large number of SNAREs (soluble N-ethylmaleimide sensitive factor attachment protein receptors) and SNARE-interacting proteins. We found that mammalian Class C Vps protein complex associated specifically with nSec-1/Munc18-a, and syntaxin 1A both in vivo and in vitro. In contrast, VAMP2 and SNAP-25, other neuronal core complex proteins, did not interact. When co-transfected with the human growth hormone (hGH) reporter gene, mammalian Class C Vps proteins enhanced Ca2+-dependent exocytosis, which was abolished by the Ca2+-channel blocker nifedipine. In hippocampal primary cultures, the lentivirus-mediated overexpression of hVps18 increased asynchronous spontaneous synaptic release without changing mEPSCs. These results indicate that mammalian Class C Vps proteins are involved in the regulation of membrane docking and fusion through an interaction with neuronal specific SNARE molecules, nSec-1/Munc18-a and syntaxin 1A. |
