Bibliographic Details
| Title: |
Synaptotagmin-1 Is an Antagonist for Munc18-1 in SNARE Zippering. |
| Authors: |
Xiaochu Lou1, Jaeil Shin1, Yoosoo Yang2, Jaewook Kim2, Yeon-Kyun Shin1 colishin@iastate.edu |
| Source: |
Journal of Biological Chemistry. 4/17/2015, Vol. 290 Issue 16, p10535-00543. 9p. |
| Subject Terms: |
*SYNAPTOTAGMINS, *CALCIUM-binding proteins, *EXOCYTOSIS, *MEMBRANE fusion, *SINGLE molecules spectra, *FLUORESCENCE |
| Abstract: |
In neuroexocytosis, SNAREs and Munc18-1 may consist of the minimal membrane fusion machinery. Consistent with this notion, we observed, using single molecule fluorescence assays, that Munc18-1 stimulates SNARE zippering and SNARE-dependent lipid mixing in the absence of a major Ca2+ sensor synaptotagmin-1 (Syt1), providing the structural basis for the conserved function of Sec1/Munc18 proteins in exocytosis. However, when full-length Syt1 is present, no enhancement of SNARE zippering and no acceleration of Ca2+-triggered content mixing by Munc18-1 are observed. Thus, our results show that Syt1 acts as an antagonist for Munc18-1 in SNARE zippering and fusion pore opening. Although the Sec1/Munc18 family may serve as part of the fusion machinery in other exocytotic pathways, Munc18-1 may have evolved to play a different role, such as regulating syntaxin-1a in neuroexocytosis. [ABSTRACT FROM AUTHOR] |
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| Database: |
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