n-Sec1: A Neural-Specific Syntaxin-Binding Protein

We have identified n-Sec1, a rat brain homolog of the yeast Sec1p protein that participates in the constitutive secretory pathway between the Golgi apparatus and the plasma membrane. The rat brain cDNA is predicted to encode a 68-kDa protein with 65% amino acid identity to Drosophila rop, 59% identi...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 91; no. 4; pp. 1445 - 1449
Main Authors Pevsner, Jonathan, Hsu, Shu-Chan, Scheller, Richard H.
Format Journal Article
LanguageEnglish
Published Washington, DC National Academy of Sciences of the United States of America 15.02.1994
National Acad Sciences
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Abstract We have identified n-Sec1, a rat brain homolog of the yeast Sec1p protein that participates in the constitutive secretory pathway between the Golgi apparatus and the plasma membrane. The rat brain cDNA is predicted to encode a 68-kDa protein with 65% amino acid identity to Drosophila rop, 59% identity to Caenorhabditis elegans unc-18, and 27% identity to Saccharomyces cerevisiae Sec1p. By RNA blot analysis, n-Sec1 mRNA expression is neural-specific. An anti-peptide antiserum directed against the n-Sec1 carboxyl terminus detects a 68-kDa protein in rat brain cytosol and membranes, but not in peripheral tissues. In the presence of syntaxin 1a, a plasma membrane protein implicated in synaptic vesicle docking, n-Sec1 becomes membrane-associated. n-Sec1 binds to syntaxin 1a, 2, and 3 fusion proteins coupled to agarose beads, but not to syntaxin 4 fusion protein or beads coupled to a variety of other proteins. These findings indicate that n-Sec1 is a neural-specific, syntaxin-binding protein that may participate in the regulation of synaptic vesicle docking and fusion.
AbstractList A rat brain homolog of the yeast Sec1p protein, which is called neural (n)-Sec1, is identified. The molecule is of particular interest because the yeast syntaxin homologs SSO1 and SSO2 were identified as multicopy suppressors of the sec1 mutation.
We have identified n-Sec1, a rat brain homolog of the yeast Sec1p protein that participates in the constitutive secretory pathway between the Golgi apparatus and the plasma membrane. The rat brain cDNA is predicted to encode a 68-kDa protein with 65% amino acid identity to Drosophila rop, 59% identity to Caenorhabditis elegans unc-18, and 27% identity to Saccharomyces cerevisiae Sec1p. By RNA blot analysis, n-Sec1 mRNA expression is neural-specific. An anti-peptide antiserum directed against the n-Sec1 carboxyl terminus detects a 68-kDa protein in rat brain cytosol and membranes, but not in peripheral tissues. In the presence of syntaxin 1a, a plasma membrane protein implicated in synaptic vesicle docking, n-Sec1 becomes membrane-associated. n-Sec1 binds to syntaxin 1a, 2, and 3 fusion proteins coupled to agarose beads, but not to syntaxin 4 fusion protein or beads coupled to a variety of other proteins. These findings indicate that n-Sec1 is a neural-specific, syntaxin-binding protein that may participate in the regulation of synaptic vesicle docking and fusion.
We have identified n-Sec1, a rat brain homolog of the yeast Sec1p protein that participates in the constitutive secretory pathway between the Golgi apparatus and the plasma membrane. The rat brain cDNA is predicted to encode a 68-kDa protein with 65% amino acid identity to Drosophila rop, 59% identity to Caenorhabditis elegans unc-18, and 27% identity to Saccharomyces cerevisiae Sec1p. By RNA blot analysis, n-Sec1 mRNA expression is neural-specific. An anti-peptide antiserum directed against the n-Sec1 carboxyl terminus detects a 68-kDa protein in rat brain cytosol and membranes, but not in peripheral tissues. In the presence of syntaxin 1a, a plasma membrane protein implicated in synaptic vesicle docking, n-Sec1 becomes membrane-associated. n-Sec1 binds to syntaxin 1a, 2, and 3 fusion proteins coupled to agarose beads, but not to syntaxin 4 fusion protein or beads coupled to a variety of other proteins. These findings indicate that n-Sec1 is a neural-specific, syntaxin-binding protein that may participate in the regulation of synaptic vesicle docking and fusion.
Author Hsu, Shu-Chan
Pevsner, Jonathan
Scheller, Richard H.
AuthorAffiliation Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University Medical Center, CA 94305
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Issue 4
Keywords Binding protein
Vertebrata
Mammalia
Neuron
Rat
Synaptic transmission
Rodentia
Neurotransmitter
Molecular cloning
Aminoacid sequence
Structural analysis
Brain (vertebrata)
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Snippet We have identified n-Sec1, a rat brain homolog of the yeast Sec1p protein that participates in the constitutive secretory pathway between the Golgi apparatus...
A rat brain homolog of the yeast Sec1p protein, which is called neural (n)-Sec1, is identified. The molecule is of particular interest because the yeast...
We have identified n-Sec1, a rat brain homolog of the yeast Sec1p protein that participates in the constitutive secretory pathway between the Golgi apparatus...
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SubjectTerms Amino Acid Sequence
Amino acids
Analytical, structural and metabolic biochemistry
Animals
Antibodies
Antigens, Surface - metabolism
Base Sequence
Binding and carrier proteins
Biological and medical sciences
Blotting, Northern
Blotting, Western
Brain
Brain Chemistry
Cell membranes
Cell-Free System
Cellular biology
Cloning, Molecular
Complementary DNA
Cytosol - chemistry
Fundamental and applied biological sciences. Psychology
Fungal Proteins - genetics
Fungal Proteins - immunology
Gels
Golgi apparatus
Membranes - chemistry
Molecular Sequence Data
Munc18 Proteins
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Neurons
Peptide Fragments - metabolism
Protein Binding
Protein Biosynthesis
Proteins
Rats
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - immunology
RNA
Rodents
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Syntaxin 1
Tissue Distribution
Transcription, Genetic
Vesicular Transport Proteins
Yeasts
Title n-Sec1: A Neural-Specific Syntaxin-Binding Protein
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Volume 91
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