Asset Details
Do you wish to reserve the book?
Reconstitution of the Vital Functions of Munc18 and Munc13 in Neurotransmitter Release
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Reconstitution of the Vital Functions of Munc18 and Munc13 in Neurotransmitter Release
Do you wish to request the book?
Reconstitution of the Vital Functions of Munc18 and Munc13 in Neurotransmitter Release
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Reconstitution of the Vital Functions of Munc18 and Munc13 in Neurotransmitter Release
2013
Overview
Neurotransmitter release depends critically on Munc18-1, Munc13, the Ca 2+ sensor synaptotagmin-1, and the soluble N-ethylmaleimide—sensitive factor (NSF) attachment protein (SNAP) receptors (SNAREs) syntaxin-1, synaptobrevin, and SNAP-25. In vitro reconstitutions have shown that syntaxin-1—SNAP-25 liposomes fuse efficiently with synaptobrevin liposomes in the presence of synaptotagmin-1—Ca 2+ , but neurotransmitter release also requires Munc18-1 and Munc13 in vivo. We found that Munc18-1 could displace SNAP-25 from syntaxin-1 and that fusion of syntaxin-1—Munc18-1 liposomes with synaptobrevin liposomes required Munc13, in addition to SNAP-25 and synaptotagmin-1-Ca 2+ . Moreover, when starting with syntaxin-1—SNAP-25 liposomes, NSF—α-SNAP disassembled the syntaxin-1—SNAP-25 heterodimers and abrogated fusion, which then required Munc18-1 and Munc13. We propose that fusion does not proceed through syntaxin-1—SNAP-25 heterodimers but starts with the syntaxin-1—Munc18-1 complex; Munc18-1 and Munc13 then orchestrate membrane fusion together with the SNAREs and synaptotagmin-1-Ca 2+ in an NSF- and SNAP-resistant manner.
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science
Subject
