Correction: Synaptic proteins promote calcium-triggered fast transition from point contact to full fusion
| Autor: | Jiajie Diao, Axel T. Brunger, Patricia Grob, Amie Nguyen, Sachi Shah, Marija Vrljic, Mark S. Padolina, Yunxiang Zhang, Eva Nogales, Ankita Shah, Ankita Srivastava, Minjoung Kyoung, Daniel J. Cipriano, Steven Chu |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Time Factors
Synaptosomal-Associated Protein 25 QH301-705.5 Vesicle-Associated Membrane Protein 2 Science Proteolipids chemistry.chemical_element Action Potentials Gene Expression Syntaxin 1 Nerve Tissue Proteins Calcium Bioinformatics Membrane Fusion Synaptic Transmission General Biochemistry Genetics and Molecular Biology Point contact Animals Biology (General) Fusion General Immunology and Microbiology Transition (genetics) General Neuroscience Correction Biological Transport General Medicine Biophysics and Structural Biology Recombinant Proteins Rats Adaptor Proteins Vesicular Transport chemistry Structural biology Synaptotagmin I Biophysics Medicine Synaptic Vesicles Neuroscience |
| Zdroj: | eLife eLife, Vol 4 (2015) |
| ISSN: | 2050-084X |
| Popis: | The molecular underpinnings of synaptic vesicle fusion for fast neurotransmitter release are still unclear. Here, we used a single vesicle-vesicle system with reconstituted SNARE and synaptotagmin-1 proteoliposomes to decipher the temporal sequence of membrane states upon Ca(2+)-injection at 250-500 μM on a 100-ms timescale. Furthermore, detailed membrane morphologies were imaged with cryo-electron microscopy before and after Ca(2+)-injection. We discovered a heterogeneous network of immediate and delayed fusion pathways. Remarkably, all instances of Ca(2+)-triggered immediate fusion started from a membrane-membrane point-contact and proceeded to complete fusion without discernible hemifusion intermediates. In contrast, pathways that involved a stable hemifusion diaphragm only resulted in fusion after many seconds, if at all. When complexin was included, the Ca(2+)-triggered fusion network shifted towards the immediate pathway, effectively synchronizing fusion, especially at lower Ca(2+)-concentration. Synaptic proteins may have evolved to select this immediate pathway out of a heterogeneous network of possible membrane fusion pathways.DOI:http://dx.doi.org/10.7554/eLife.00109.001. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|