Journal
STRUCTURE
Volume 19, Issue 10, Pages 1443-1455Publisher
CELL PRESS
DOI: 10.1016/j.str.2011.07.012
Keywords
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Funding
- US Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]
- American Heart Association
- Welch foundation [I-1304]
- NIH [NS37200]
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Unc13/MunC13s play a crucial function in neurotransmitter release through their MUN domain, which mediates the transition from the Syntaxin-1/Munc18-1 complex to the SNARE complex. The MUN domain was suggested to be related to tethering factors, but no MUN-domain structure is available to experimentally validate this notion and address key unresolved questions about the interactions and minimal structural unit required for Unc13/Munc13 function. Here we identify an autonomously folded module within the MUN domain (MUN-CD) and show that its crystal structure is remarkably similar to several tethering factors. We also show that the activity in promoting the Syntaxin-1/Munc18-1 to SNARE complex transition is strongly impaired in MUN-CD. These results show that MUN domains and tethering factors indeed belong to the same family and may have a common role in membrane trafficking. We propose a model whereby the MUN-CD module is central for Munc13 function but full activity requires adjacent sequences.
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