A Gain-of-Function Mutation in Synaptotagmin-1 Reveals a Critical Role of Ca -Dependent Soluble N-Ethylmaleimide-Sensitive Factor Attachment Protein Receptor Complex Binding in Synaptic Exocytosis
نویسندگان
چکیده
Zhiping P. Pang,1* Ok-Ho Shin,1* Alexander C. Meyer,4* Christian Rosenmund,4,5 and Thomas C. Südhof1,2,3 1Center for Basic Neuroscience, 2Department of Molecular Genetics, and 3Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390, 4Department of Membrane Biophysics, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany, and 5Departments of Neuroscience and Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030
منابع مشابه
A gain-of-function mutation in synaptotagmin-1 reveals a critical role of Ca2+-dependent soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex binding in synaptic exocytosis.
Synaptotagmin-1, the Ca2+ sensor for fast neurotransmitter release, was proposed to function by Ca2+-dependent phospholipid binding and/or by Ca2+-dependent soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex binding. Extensive in vivo data support the first hypothesis, but testing the second hypothesis has been difficult because no synaptotagmin-1 mutation is ...
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Syntaxin-1 is a component of the synaptic vesicle docking and/or membrane fusion soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) complex (7S and 20S complexes) in nerve terminals. Syntaxin-1 also forms a heterodimer with Munc18/n-Sec1/rbSec1 in a complex that is distinct from the 7S and 20S complexes. In this report, we identify a novel syntaxin-1-binding protein, tomosyn,...
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تاریخ انتشار 2006