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  • 1
    Publication Date: 2016-02-26
    Description: Synaptic transmission is mediated by the release of neurotransmitters, which involves exo-endocytotic cycling of synaptic vesicles. To maintain synaptic function, synaptic vesicles are refilled with thousands of neurotransmitter molecules within seconds after endocytosis, using the energy provided by an electrochemical proton gradient. However, it is unclear how transmitter molecules carrying different net charges can be efficiently sequestered while maintaining charge neutrality and osmotic balance. We used single-vesicle imaging to monitor pH and electrical gradients and directly showed different uptake mechanisms for glutamate and gamma-aminobutyric acid (GABA) operating in parallel. In contrast to glutamate, GABA was exchanged for protons, with no other ions participating in the transport cycle. Thus, only a few components are needed to guarantee reliable vesicle filling with different neurotransmitters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Farsi, Zohreh -- Preobraschenski, Julia -- van den Bogaart, Geert -- Riedel, Dietmar -- Jahn, Reinhard -- Woehler, Andrew -- New York, N.Y. -- Science. 2016 Feb 26;351(6276):981-4. doi: 10.1126/science.aad8142. Epub 2016 Feb 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany. ; Department of Tumor Immunology, Radboud University Medical Center, 6525GA Nijmegen, Netherlands. ; Laboratory of Electron Microscopy, Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany. ; Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany. rjahn@gwdg.de. ; Department of Membrane Biophysics, Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany. Deutsche Forschungsgemeinschaft (DFG) Research Center for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB), Gottingen, 37073, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26912364" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2012-06-02
    Description: Cellular membrane fusion is thought to proceed through intermediates including docking of apposed lipid bilayers, merging of proximal leaflets to form a hemifusion diaphragm, and fusion pore opening. A membrane-bridging four-helix complex of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) mediates fusion. However, how assembly of the SNARE complex generates docking and other fusion intermediates is unknown. Using a cell-free reaction, we identified intermediates visually and then arrested the SNARE fusion machinery when fusion was about to begin. Partial and directional assembly of SNAREs tightly docked bilayers, but efficient fusion and an extended form of hemifusion required assembly beyond the core complex to the membrane-connecting linkers. We propose that straining of lipids at the edges of an extended docking zone initiates fusion.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677693/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677693/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hernandez, Javier M -- Stein, Alexander -- Behrmann, Elmar -- Riedel, Dietmar -- Cypionka, Anna -- Farsi, Zohreh -- Walla, Peter J -- Raunser, Stefan -- Jahn, Reinhard -- 3P01GM072694-05S1/GM/NIGMS NIH HHS/ -- P01 GM072694/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Jun 22;336(6088):1581-4. doi: 10.1126/science.1221976. Epub 2012 May 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22653732" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Lipid Bilayers/chemistry/*metabolism ; *Liposomes/chemistry/metabolism ; *Membrane Fusion ; Protein Binding ; Protein Conformation ; Rats ; SNARE Proteins/chemistry/*metabolism ; Vesicle-Associated Membrane Protein 2/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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