Výsledky vyhledávání - "Andrea, Scheutzow"

Arrangements of proteins at reconstituted synaptic vesicle fusion sites depend on membrane separation

Autor: Thomas H. Söllner, Dustin R. Morado, Lucy Ginger, John A. G. Briggs, Andrea Scheutzow, Andreas F.-P. Sonnen, Joerg Malsam

Publikováno v: Febs Letters
FEBS Letters

Synaptic vesicle proteins, including N‐ethylmaleimide‐sensitive factor attachment protein receptors (SNAREs), Synaptotagmin‐1 and Complexin, are responsible for controlling the synchronised fusion of synaptic vesicles with the presynaptic plasm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::617bb5b809e94665efcfcc8f457bdc12
https://doi.org/10.1002/1873-3468.13916

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Complexin suppresses spontaneous exocytosis by capturing the membrane-proximal regions of VAMP2 and SNAP25

Autor: Joerg Malsam, Fereshteh Zarebidaki, Andreas F.-P. Sonnen, Irmgard Sinning, Christian Rosenmund, Andrea Scheutzow, Simon Baerfuss, Klemens Wild, Thomas H. Soellner, John A. G. Briggs, Thorsten Trimbuch

SummaryThe neuronal protein complexin contains multiple domains that exert both clamping and facilitatory functions to tune spontaneous and action potential triggered synaptic release. We address the clamping mechanism and show that the accessory hel

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cd25a930b6e9883f7c131ae6e7b2222
https://doi.org/10.1101/849885

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Complexin Suppresses Spontaneous Exocytosis by Capturing the Membrane-Proximal Regions of VAMP2 and SNAP25

Autor: Lukas Rohland, Irmgard Sinning, John A. G. Briggs, Thorsten Trimbuch, Klemens Wild, Simon Bärfuss, Fereshteh Zarebidaki, Andreas F.-P. Sonnen, Christian Rosenmund, Matthias P. Mayer, Thomas H. Söllner, Andrea Scheutzow, Jörg Malsam

Publikováno v: Cell reports
Cell Reports

Summary The neuronal protein complexin contains multiple domains that exert clamping and facilitatory functions to tune spontaneous and action potential-triggered synaptic release. We address the clamping mechanism and show that the accessory helix o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78f5799250257592d7ff5b5ae392d6b3
https://pubmed.ncbi.nlm.nih.gov/32698012

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Interactions Between SNAP-25 and Synaptotagmin-1 Are Involved in Vesicle Priming, Clamping Spontaneous and Stimulating Evoked Neurotransmission

Autor: Andrea Scheutzow, Keimpe D. Wierda, Jakob B. Sørensen, Jörg Malsam, Thomas H. Söllner, Melanie Schupp, Marvin Ruiter

Publikováno v: The Journal of Neuroscience. 36:11865-11880

Whether interactions between synaptotagmin-1 (syt-1) and the soluble NSF attachment protein receptors (SNAREs) are required during neurotransmission is debated. We examined five SNAP-25 mutations designed to interfere with syt-1 interactions. One mut

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98901948b0cd9bf746ac4927ed00e541
https://doi.org/10.1523/jneurosci.1011-16.2016

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An Electrostatic Energy Barrier for SNARE-Dependent Spontaneous and Evoked Synaptic Transmission

Autor: Anna Kádková, Thomas H. Söllner, Marvin Ruiter, Jörg Malsam, Andrea Scheutzow, Jakob B. Sørensen

Publikováno v: Ruiter, M, Kádková, A, Scheutzow, A, Malsam, J, Söllner, T H & Sørensen, J B 2019, ' An Electrostatic Energy Barrier for SNARE-Dependent Spontaneous and Evoked Synaptic Transmission ', Cell Reports, vol. 26, no. 9, pp. 2340-2352, e1-e5 . https://doi.org/10.1016/j.celrep.2019.01.103

Information transfer across CNS synapses depends on the very low basal vesicle fusion rate and the ability to rapidly upregulate that rate upon Ca2+ influx. We show that local electrostatic repulsion participates in creating an energy barrier, which

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a791034a2cde8ecb3e8d02e85e95001
https://pubmed.ncbi.nlm.nih.gov/30811985

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SNAREpin Assembly by Munc18-1 Requires Previous Vesicle Docking by Synaptotagmin 1

Autor: Thomas H. Söllner, Joerg Malsam, Jean Michel Krause, Daniel Parisotto, Andrea Scheutzow

Publikováno v: Journal of Biological Chemistry. 287:31041-31049

Regulated exocytosis requires the general membrane fusion machinery-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) and Sec1/Munc18 (SM) proteins. Using reconstituted giant unilamellar vesicles containing preassembled t-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a45b6c5d1a43668e60f738b03ae9f10b
https://doi.org/10.1074/jbc.m112.386805

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Complexin arrests a pool of docked vesicles for fast Ca2+-dependent release

Autor: Daniel Parisotto, Thomas H. Söllner, John A. G. Briggs, Tanmay A.M. Bharat, Jean Michel Krause, Andrea Scheutzow, Jörg Malsam

Publikováno v: The EMBO Journal. 31:3270-3281

Regulated exocytosis requires that the assembly of the basic membrane fusion machinery is temporarily arrested. Synchronized membrane fusion is then caused by a specific trigger—a local rise of the Ca 2+ concentration. Using reconstituted giant uni

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e531cbcd53f438b550a6fd99898e31a9
https://doi.org/10.1038/emboj.2012.164

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A Post-Docking Role of Synaptotagmin 1-C2B Domain Bottom Residues R398/399 in Mouse Chromaffin Cells

Autor: Thomas H. Söllner, Andrea Scheutzow, J. R. T. van Weering, H. de Wit, Jörg Malsam, G. H. Kedar, A. S. Munch, Matthijs Verhage, Sébastien Houy, Bassam Tawfik, Jakob B. Sørensen

Publikováno v: Journal of Neuroscience, 35(42), 14172-14182. Society for Neuroscience
The Journal of Neuroscience, 35(42), 14172-14182. Society for Neuroscience
Kedar, G H, Munch, A S, van Weering, J R T, Malsam, J, Scheutzow, A, de Wit, H, Houy, S, Tawfik, B, Sollner, T H, Sorensen, J B & Verhage, M 2015, ' A Post-Docking Role of Synaptotagmin 1-C2B Domain Bottom Residues R398/399 in Mouse Chromaffin Cells. ', The Journal of Neuroscience, vol. 35, no. 42, pp. 14172-14182 . https://doi.org/10.1523/JNEUROSCI.1911-15.2015
Kedar, G H, Munch, A S, van Weering, J R T, Malsam, J, Scheutzow, A, de Wit, H, Houy, S, Tawfik, B, Sollner, T H, Sorensen, J B & Verhage, M 2015, ' A Post-Docking Role of Synaptotagmin 1-C2B Domain Bottom Residues R398/399 in Mouse Chromaffin Cells. ', Journal of Neuroscience, vol. 35, no. 42, pp. 14172-14182 . https://doi.org/10.1523/JNEUROSCI.1911-15.2015

Synaptotagmin-1 (Syt1) is the principal Ca2+sensor for vesicle fusion and is also essential for vesicle docking in chromaffin cells. Docking depends on interactions of the Syt1-C2B domain with the t-SNARE SNAP25/Syntaxin1 complex and/or plasma membra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d8b510f6276b899af4563f83e5a5d02
https://research.vumc.nl/en/publications/44f97e77-2f0d-4271-b996-ff95c1fb7c6e

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An Extended Helical Conformation in Domain 3a of Munc18-1 Provides a Template for SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Complex Assembly*

Autor: Thomas H. Söllner, Joerg Malsam, Maximilian Pfau, Daniel Parisotto, Matthias P. Mayer, Andrea Scheutzow, Klemens Wild, Irmgard Sinning

Munc18-1, a SEC1/Munc18 protein and key regulatory protein in synaptic transmission, can either promote or inhibit SNARE complex assembly. Although the binary inhibitory interaction between Munc18-1 and closed syntaxin 1 is well described, the mechan

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::240b240c832a1b05d59f2ad88a1000e6
https://europepmc.org/articles/PMC3975013/

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SNARE and regulatory proteins induce local membrane protrusions to prime docked vesicles for fast calcium-triggered fusion

Autor: Thomas H. Söllner, John A. G. Briggs, Jörg Malsam, Andrea Scheutzow, Wim J. H. Hagen, Tanmay A.M. Bharat

Publikováno v: EMBO reports. 15(3)

Synaptic vesicles fuse with the plasma membrane in response to Ca(2+) influx, thereby releasing neurotransmitters into the synaptic cleft. The protein machinery that mediates this process, consisting of soluble N-ethylmaleimide-sensitive factor attac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8237edb24cbc919bf490f3bd60d074e
https://pubmed.ncbi.nlm.nih.gov/24493260

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