Abstract
Syntaxin 1 is a SNARE protein that plays a central role in synaptic vesicle (SV) exocytosis. We generated an antibody that specifically recognizes a casein kinase II-mediated phosphorylation on serine-14 of syntaxin 1. In this report we show that this phosphorylation occurs in vivo and is developmentally regulated in the rat brain, rising to a level of 40% of the total syntaxin in adult animals. Phosphorylated syntaxin is preferentially associated with SNAP-25 and localizes to discrete domains of the axonal plasma membrane that do not colocalize with pools of synaptic vesicles. These phosphosyntaxin domains may define fusion sites for a novel class of vesicles outside classical active zones.
MeSH terms
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Amino Acid Sequence
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Animals
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Antibodies
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Antibody Specificity
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Antigens, Surface / analysis
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Antigens, Surface / chemistry
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Antigens, Surface / metabolism*
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Axons / metabolism*
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Axons / ultrastructure
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Brain / metabolism*
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Brain / ultrastructure
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Brain Chemistry
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Casein Kinase II
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Image Processing, Computer-Assisted
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Nerve Tissue Proteins / analysis
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Nerve Tissue Proteins / chemistry
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Nerve Tissue Proteins / metabolism*
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Phosphorylation
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Protein Serine-Threonine Kinases / metabolism
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Rats
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Syntaxin 1
Substances
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Antibodies
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Antigens, Surface
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Nerve Tissue Proteins
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Recombinant Proteins
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Stx1a protein, rat
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Syntaxin 1
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Casein Kinase II
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Protein Serine-Threonine Kinases