دورية أكاديمية
أعرض في EDS

Munc13 C2B domain is an activity-dependent Ca2+ regulator of synaptic exocytosis.

التفاصيل البيبلوغرافية
العنوان: Munc13 C2B domain is an activity-dependent Ca2+ regulator of synaptic exocytosis.
المؤلفون: Shin OH; Department of Neuroscience, University of Texas Southwestern Medical Center, Dallas, Texas, USA., Lu J, Rhee JS, Tomchick DR, Pang ZP, Wojcik SM, Camacho-Perez M, Brose N, Machius M, Rizo J, Rosenmund C, Südhof TC
المصدر: Nature structural & molecular biology [Nat Struct Mol Biol] 2010 Mar; Vol. 17 (3), pp. 280-8. Date of Electronic Publication: 2010 Feb 14.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Nature Pub. Group Country of Publication: United States NLM ID: 101186374 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1545-9985 (Electronic) Linking ISSN: 15459985 NLM ISO Abbreviation: Nat Struct Mol Biol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: New York : Nature Pub. Group, c2004-
مواضيع طبية MeSH: Calcium/*metabolism , Exocytosis/*physiology , Nerve Tissue Proteins/*chemistry , Nerve Tissue Proteins/*metabolism , Synaptic Transmission/*physiology , Synaptic Vesicles/*metabolism, Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; Electrophysiology ; Exocytosis/genetics ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Nerve Tissue Proteins/genetics ; Phospholipids ; Protein Structure, Tertiary/genetics ; Rats ; Sequence Homology, Amino Acid ; Spectrometry, Fluorescence ; Synaptic Transmission/genetics ; Synaptic Vesicles/genetics
مستخلص: Munc13 is a multidomain protein present in presynaptic active zones that mediates the priming and plasticity of synaptic vesicle exocytosis, but the mechanisms involved remain unclear. Here we use biophysical, biochemical and electrophysiological approaches to show that the central C(2)B domain of Munc13 functions as a Ca(2+) regulator of short-term synaptic plasticity. The crystal structure of the C(2)B domain revealed an unusual Ca(2+)-binding site with an amphipathic alpha-helix. This configuration confers onto the C(2)B domain unique Ca(2+)-dependent phospholipid-binding properties that favor phosphatidylinositolphosphates. A mutation that inactivated Ca(2+)-dependent phospholipid binding to the C(2)B domain did not alter neurotransmitter release evoked by isolated action potentials, but it did depress release evoked by action-potential trains. In contrast, a mutation that increased Ca(2+)-dependent phosphatidylinositolbisphosphate binding to the C(2)B domain enhanced release evoked by isolated action potentials and by action-potential trains. Our data suggest that, during repeated action potentials, Ca(2+) and phosphatidylinositolphosphate binding to the Munc13 C(2)B domain potentiate synaptic vesicle exocytosis, thereby offsetting synaptic depression induced by vesicle depletion.
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معلومات مُعتمدة: NS40944 United States NS NINDS NIH HHS; R01 NS051262 United States NS NINDS NIH HHS; R01 NS040944 United States NS NINDS NIH HHS; NS051262 United States NS NINDS NIH HHS; United States HHMI Howard Hughes Medical Institute
فهرسة مساهمة: Indexing Agency: NLM Local ID #: HHMIMS223272.
سلسلة جزيئية: PDB 3KWT; 3KWU
المشرفين على المادة: 0 (Nerve Tissue Proteins)
0 (Phospholipids)
0 (Unc13a protein, rat)
SY7Q814VUP (Calcium)
تواريخ الأحداث: Date Created: 20100216 Date Completed: 20100511 Latest Revision: 20230425
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC2916016
DOI: 10.1038/nsmb.1758
PMID: 20154707
قاعدة البيانات: MEDLINE
الوصف
تدمد:1545-9985
DOI:10.1038/nsmb.1758