دورية أكاديمية
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Mechanistic insights into neurotransmitter release and presynaptic plasticity from the crystal structure of Munc13-1 C 1 C 2 BMUN.

التفاصيل البيبلوغرافية
العنوان: Mechanistic insights into neurotransmitter release and presynaptic plasticity from the crystal structure of Munc13-1 C 1 C 2 BMUN.
المؤلفون: Xu J; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, United States.; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States., Camacho M; Department of Neurophysiology, NeuroCure Cluster of Excellence, Charité-Universitätsmedizin Berlin, Berlin, Germany., Xu Y; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, United States.; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States., Esser V; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, United States.; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States., Liu X; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, United States.; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States., Trimbuch T; Department of Neurophysiology, NeuroCure Cluster of Excellence, Charité-Universitätsmedizin Berlin, Berlin, Germany., Pan YZ; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, United States.; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States., Ma C; Key Laboratory of Molecular Biophysics of the Ministry of Education, Huazhong University of Science and Technology, Wuhan, China.; College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China., Tomchick DR; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, United States.; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States., Rosenmund C; Department of Neurophysiology, NeuroCure Cluster of Excellence, Charité-Universitätsmedizin Berlin, Berlin, Germany., Rizo J; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, United States.; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States.
المصدر: ELife [Elife] 2017 Feb 08; Vol. 6. Date of Electronic Publication: 2017 Feb 08.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012-
مواضيع طبية MeSH: Nerve Tissue Proteins/*chemistry , Nerve Tissue Proteins/*metabolism , Neurotransmitter Agents/*metabolism, Animals ; Cells, Cultured ; Crystallography, X-Ray ; Mice ; Models, Molecular ; Neurons/physiology ; Protein Conformation ; Rats
مستخلص: Munc13-1 acts as a master regulator of neurotransmitter release, mediating docking-priming of synaptic vesicles and diverse presynaptic plasticity processes. It is unclear how the functions of the multiple domains of Munc13-1 are coordinated. The crystal structure of a Munc13-1 fragment including its C 1 , C 2 B and MUN domains (C 1 C 2 BMUN) reveals a 19.5 nm-long multi-helical structure with the C 1 and C 2 B domains packed at one end. The similar orientations of the respective diacyglycerol- and Ca 2+ -binding sites of the C 1 and C 2 B domains suggest that the two domains cooperate in plasma-membrane binding and that activation of Munc13-1 by Ca 2+ and diacylglycerol during short-term presynaptic plasticity are closely interrelated. Electrophysiological experiments in mouse neurons support the functional importance of the domain interfaces observed in C 1 C 2 BMUN. The structure imposes key constraints for models of neurotransmitter release and suggests that Munc13-1 bridges the vesicle and plasma membranes from the periphery of the membrane-membrane interface.
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معلومات مُعتمدة: R01 NS037200 United States NS NINDS NIH HHS; R01 NS040944 United States NS NINDS NIH HHS; R35 NS097333 United States NS NINDS NIH HHS
فهرسة مساهمة: Keywords: Munc13; biophysics; calcium binding; mouse; neuroscience; neurotransmitter release; presynaptic plasticity; structural biology; synaptic vesicle fusion
المشرفين على المادة: 0 (Nerve Tissue Proteins)
0 (Neurotransmitter Agents)
0 (Unc13a protein, mouse)
تواريخ الأحداث: Date Created: 20170209 Date Completed: 20180207 Latest Revision: 20181113
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC5344669
DOI: 10.7554/eLife.22567
PMID: 28177287
قاعدة البيانات: MEDLINE
الوصف
تدمد:2050-084X
DOI:10.7554/eLife.22567