A VAMP-binding protein from Aplysia required for neurotransmitter release

Science. 1995 Sep 15;269(5230):1580-3. doi: 10.1126/science.7667638.

Abstract

Before the fusion of synaptic vesicles with the plasma membrane, a protein complex is thought to form between VAMP--an integral membrane protein of the vesicle--and two proteins associated with the plasma membrane, SNAP-25 and syntaxin. The yeast two-hybrid interaction cloning system has now been used to identify additional proteins from Aplysia that interact directly with VAMP. A 33-kilodalton membrane protein, termed VAP-33 (VAMP-associated protein of 33 kilodaltons), was identified whose corresponding messenger RNA was detected only in the central nervous system and the gill of Aplysia. Presynaptic injection of antibodies specific for VAP-33 inhibited synaptic transmission, which suggests that VAP-33 is required for the exocytosis of neurotransmitter.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aplysia
  • Base Sequence
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / physiology*
  • Cells, Cultured
  • Central Nervous System / chemistry
  • Cloning, Molecular
  • Exocytosis
  • Gills / innervation
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Membrane Proteins / physiology*
  • Molecular Sequence Data
  • Molecular Weight
  • Motor Neurons / physiology
  • Nerve Tissue Proteins / metabolism*
  • Neurons / physiology*
  • Neurons, Afferent / physiology
  • Neurotransmitter Agents / metabolism*
  • R-SNARE Proteins
  • Synaptic Transmission*
  • Synaptic Vesicles / physiology
  • Vesicular Transport Proteins*

Substances

  • Carrier Proteins
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Neurotransmitter Agents
  • R-SNARE Proteins
  • VAPA protein, human
  • Vesicular Transport Proteins

Associated data

  • GENBANK/U36779