Munc-18 (an acronym for mammalian uncoordinated-18) proteins are the mammalian homologue of UNC-18 (which was first discovered in the nematode worm C. elegans [1] [2]) and are a member of the Sec1/Munc18-like (SM) protein family.

Sep 23, 2019 · Munc18-1 and Munc13-1 orchestrate SNARE complex formation by an NSF-SNAP-resistant mechanism 11 whereby Munc18-1 first binds to a self-inhibited “closed” conformation of syntaxin-1 12,13 (Fig...

Munc-18 is thought to serve multiple roles in exocytosis, the first being as an inhibitory protein which prevents assembly of the SNARE complex at inopportune times and which plays an important role in mediating vesicle docking (de Wit, 2010; Dulubova et al., 1999; Toonen et al., 2006; Voets et al., 2001; Wojcik and Brose, 2007; Yang et al., 2000).

Munc-18-1 regulates the initial release rate of exocytosis. Biophys J. 2008;94:1084–1093. doi: 10.1529/biophysj.107.111203. [ DOI ] [ PMC free article ] [ PubMed ] [ Google Scholar ]

Mammalian uncoordinated-18 (Munc 18) protein belongs to family of the Sec1/Munc18-like (SM) proteins. The Munc-18 protein is considered as essential component of trans-SNARE complex crucial for the exocytosis of secretory granules ( Zilly et al., 2006 ).

Jan 8, 2019 · Acceptor liposomes (Munc18-1/Syx1) contain 55% POPC, 20% POPE, 18% DOPS, 2% PIP2, and 5% DAG.

Nov 30, 2017 · Based on the reports of gene abnormalities including haploinsufficiency and heterozygous mutations, an essential role of MUNC-18-1 has been predicted in the etiology of early infantile epileptic encephalopathy with suppression-burst (EIEE; Ohtahara syndrome) and other neurodevelopmental disorders such as neonatal epileptic encephalopathy (NEE ...

Munc-18-1 is a 67-kDa neuronal protein that binds tightly to syntaxin 1 and functions in synaptic vesicle exocytosis (Hata, Y., Slaughter, C. A., and Südhof, T. C. (1993a) Nature 366, 347-351). We have now characterized a new Munc-18 isoform, Munc-18-2, that exhibits 63% amino acid sequence identity with Munc-18-1.

Munc-18-1 is crucial for vesicle exocytosis at presynaptic terminals (Verhage et al., 2000) and undergoes rapid PKC-catalyzed phosphorylation during the depolarization stage (Craig et al., 2003; de Vries et al., 2000).

Synaptic transmission of neuronal information is regulated by a series of key proteins, among which mammalian uncoordinated 18 (Munc18) is one class of the important proteins for synaptic membrane fusion.