Cargando…
Focused clamping of a single neuronal SNARE complex by complexin under high mechanical tension
Neuronal soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) catalyze synaptic vesicle fusion with presynaptic membranes through the formation of SNARE complexes. Complexin (Cpx) is the only presynaptic protein that tightly binds to SNAREs and regulates membrane fusion, b...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6128827/ https://www.ncbi.nlm.nih.gov/pubmed/30194295 http://dx.doi.org/10.1038/s41467-018-06122-3 |
_version_ | 1783353701679759360 |
---|---|
author | Shon, Min Ju Kim, Haesoo Yoon, Tae-Young |
author_facet | Shon, Min Ju Kim, Haesoo Yoon, Tae-Young |
author_sort | Shon, Min Ju |
collection | PubMed |
description | Neuronal soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) catalyze synaptic vesicle fusion with presynaptic membranes through the formation of SNARE complexes. Complexin (Cpx) is the only presynaptic protein that tightly binds to SNAREs and regulates membrane fusion, but how it modulates the energy landscape of SNARE complex assembly, especially under mechanical tension on the complex, remains unclear. Here, using magnetic tweezers, we report how Cpx interacts with single SNARE complexes. The effects of Cpx manifest only under high mechanical tensions above 13 pN. Cpx stabilizes the central four-helix bundle of SNARE motifs and, at the same time, prevents the complete zippering of SNAREs by inhibiting linker-domain assembly. These results suggest that Cpx generates a focused clamp for the neuronal SNARE complex in a linker-open conformation. Our results provide a hint as to how Cpx cooperates with neuronal SNAREs to prime synaptic vesicles in preparation for synchronous neurotransmitter release. |
format | Online Article Text |
id | pubmed-6128827 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-61288272018-09-10 Focused clamping of a single neuronal SNARE complex by complexin under high mechanical tension Shon, Min Ju Kim, Haesoo Yoon, Tae-Young Nat Commun Article Neuronal soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) catalyze synaptic vesicle fusion with presynaptic membranes through the formation of SNARE complexes. Complexin (Cpx) is the only presynaptic protein that tightly binds to SNAREs and regulates membrane fusion, but how it modulates the energy landscape of SNARE complex assembly, especially under mechanical tension on the complex, remains unclear. Here, using magnetic tweezers, we report how Cpx interacts with single SNARE complexes. The effects of Cpx manifest only under high mechanical tensions above 13 pN. Cpx stabilizes the central four-helix bundle of SNARE motifs and, at the same time, prevents the complete zippering of SNAREs by inhibiting linker-domain assembly. These results suggest that Cpx generates a focused clamp for the neuronal SNARE complex in a linker-open conformation. Our results provide a hint as to how Cpx cooperates with neuronal SNAREs to prime synaptic vesicles in preparation for synchronous neurotransmitter release. Nature Publishing Group UK 2018-09-07 /pmc/articles/PMC6128827/ /pubmed/30194295 http://dx.doi.org/10.1038/s41467-018-06122-3 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Shon, Min Ju Kim, Haesoo Yoon, Tae-Young Focused clamping of a single neuronal SNARE complex by complexin under high mechanical tension |
title | Focused clamping of a single neuronal SNARE complex by complexin under high mechanical tension |
title_full | Focused clamping of a single neuronal SNARE complex by complexin under high mechanical tension |
title_fullStr | Focused clamping of a single neuronal SNARE complex by complexin under high mechanical tension |
title_full_unstemmed | Focused clamping of a single neuronal SNARE complex by complexin under high mechanical tension |
title_short | Focused clamping of a single neuronal SNARE complex by complexin under high mechanical tension |
title_sort | focused clamping of a single neuronal snare complex by complexin under high mechanical tension |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6128827/ https://www.ncbi.nlm.nih.gov/pubmed/30194295 http://dx.doi.org/10.1038/s41467-018-06122-3 |
work_keys_str_mv | AT shonminju focusedclampingofasingleneuronalsnarecomplexbycomplexinunderhighmechanicaltension AT kimhaesoo focusedclampingofasingleneuronalsnarecomplexbycomplexinunderhighmechanicaltension AT yoontaeyoung focusedclampingofasingleneuronalsnarecomplexbycomplexinunderhighmechanicaltension |