Abstract
Syntaxins are thought to function during vesicular transport as receptors on the target membrane and to contribute to the specificity of membrane docking and fusion by interacting with vesicle-associated receptors. Here, syntaxin 5 (Syn5) was shown to be an integral component of endoplasmic reticulum-derived transport vesicles. This pool, but not the target, Golgi-associated Syn5 pool, was essential for the assembly of vesicular-tubular pre-Golgi intermediates and the delivery of cargo to the Golgi. The requirement for vesicle-associated Syn5 in transport suggests a reevaluation of the basis for operation of the early secretory pathway.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphate / metabolism
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Animals
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Antibodies
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Biological Transport
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Carrier Proteins / metabolism
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Cell Line
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Endoplasmic Reticulum / metabolism*
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Golgi Apparatus / metabolism*
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Golgi Apparatus / ultrastructure
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Mannose-Binding Lectins
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Membrane Fusion
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Membrane Glycoproteins*
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Membrane Proteins / immunology
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Membrane Proteins / metabolism*
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N-Ethylmaleimide-Sensitive Proteins
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Organelles / metabolism
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Qa-SNARE Proteins
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Qb-SNARE Proteins
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Qc-SNARE Proteins
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R-SNARE Proteins
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Rats
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SNARE Proteins
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Vesicular Transport Proteins*
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Vesicular stomatitis Indiana virus / physiology
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Viral Envelope Proteins / metabolism
Substances
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Antibodies
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BET1 protein, rat
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Carrier Proteins
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G protein, vesicular stomatitis virus
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Gosr2 protein, rat
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LMAN1 protein, human
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Mannose-Binding Lectins
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Membrane Glycoproteins
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Membrane Proteins
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Qa-SNARE Proteins
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Qb-SNARE Proteins
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Qc-SNARE Proteins
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R-SNARE Proteins
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SNARE Proteins
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Sec22a protein, rat
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Vesicular Transport Proteins
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Viral Envelope Proteins
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Adenosine Triphosphate
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N-Ethylmaleimide-Sensitive Proteins
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Nsf protein, rat