Analysis of regulated exocytosis in adrenal chromaffin cells: insights into NSF/SNAP/SNARE function

Bioessays. 1998 Apr;20(4):328-35. doi: 10.1002/(SICI)1521-1878(199804)20:4<328::AID-BIES9>3.0.CO;2-L.

Abstract

Many of the proteins that function in regulated exocytosis have now been identified. Several proteins form part of a conserved core machinery that acts in many intracellular vesicular fusion steps and their essential roles confirmed by molecular genetic analysis. In addition, studies with adrenal chromaffin and PC12 cells have demonstrated the function of various proteins in regulated exocytosis and have permitted dissection of the stages of exocytosis in which they act. N-Ethylmaleimide-sensitive fusion protein (NSF) and soluble NSF attachment proteins (SNAPs) are key proteins in exocytosis. Examination of their function has indicated that they have a predocking role most likely as molecular chaperones to prepare the docking/fusion machinery. The exact site and time of action in exocytosis of many of the other identified proteins are unknown. A major emphasis for the future will be analysis of the molecular physiology of regulated exocytosis to permit the assignment of functions to identified proteins in particular stages of the regulated exocytotic pathway.

Publication types

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

MeSH terms

  • Adrenal Medulla / cytology*
  • Adrenal Medulla / metabolism
  • Animals
  • Carrier Proteins / physiology*
  • Exocytosis / physiology*
  • Membrane Proteins / physiology*
  • Models, Biological
  • Molecular Chaperones / physiology*
  • N-Ethylmaleimide-Sensitive Proteins
  • Nerve Tissue Proteins / physiology*
  • PC12 Cells / metabolism
  • R-SNARE Proteins
  • Rats
  • SNARE Proteins
  • Synaptosomal-Associated Protein 25
  • Vesicular Transport Proteins*

Substances

  • Carrier Proteins
  • Membrane Proteins
  • Molecular Chaperones
  • Nerve Tissue Proteins
  • R-SNARE Proteins
  • SNARE Proteins
  • Snap25 protein, rat
  • Synaptosomal-Associated Protein 25
  • Vesicular Transport Proteins
  • N-Ethylmaleimide-Sensitive Proteins
  • Nsf protein, rat