Role of vesicle-associated syntaxin 5 in the assembly of pre-Golgi intermediates

Science. 1998 Jan 30;279(5351):696-700. doi: 10.1126/science.279.5351.696.

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

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Antibodies
  • Biological Transport
  • Carrier Proteins / metabolism
  • Cell Line
  • Endoplasmic Reticulum / metabolism*
  • Golgi Apparatus / metabolism*
  • Golgi Apparatus / ultrastructure
  • Mannose-Binding Lectins
  • Membrane Fusion
  • Membrane Glycoproteins*
  • Membrane Proteins / immunology
  • Membrane Proteins / metabolism*
  • N-Ethylmaleimide-Sensitive Proteins
  • Organelles / metabolism
  • Qa-SNARE Proteins
  • Qb-SNARE Proteins
  • Qc-SNARE Proteins
  • R-SNARE Proteins
  • Rats
  • SNARE Proteins
  • Vesicular Transport Proteins*
  • Vesicular stomatitis Indiana virus / physiology
  • Viral Envelope Proteins / metabolism

Substances

  • Antibodies
  • BET1 protein, rat
  • Carrier Proteins
  • G protein, vesicular stomatitis virus
  • Gosr2 protein, rat
  • LMAN1 protein, human
  • Mannose-Binding Lectins
  • Membrane Glycoproteins
  • Membrane Proteins
  • Qa-SNARE Proteins
  • Qb-SNARE Proteins
  • Qc-SNARE Proteins
  • R-SNARE Proteins
  • SNARE Proteins
  • Sec22a protein, rat
  • Vesicular Transport Proteins
  • Viral Envelope Proteins
  • Adenosine Triphosphate
  • N-Ethylmaleimide-Sensitive Proteins
  • Nsf protein, rat