Mechanisms of exocytosis

Acta Physiol (Oxf). 2008 Feb;192(2):185-93. doi: 10.1111/j.1748-1716.2007.01803.x. Epub 2007 Nov 15.

Abstract

Catecholamines and peptides secreted from dense-core vesicles (DCVs) of adrenal chromaffin cells regulate a wide variety of physiological processes. For instance, the release of noradrenaline and adrenaline plays a key role in regulating heart rate and blood pressure. Thus understanding the mechanisms of secretory processes of DCVs is crucial for understanding the basis of diseases such as hypertension. DCVs undergo several stages of secretory processing before they are exocytosed. These include docking, priming and triggering of membrane fusion/exocytosis. Molecular studies of DCV exocytosis have identified many proteins critically involved in DCV secretion. These proteins include SNARE proteins, Munc18-1, phosphatidylinositol transfer protein, type I phosphatidylinositol-4-phosphate-5-kinases, NSF, Munc13, CAPS1, synaptotagmins, RalA/RalB GTPases and exocyst proteins. In this article, I will discuss the functions of these proteins within the context of the stages (i.e. docking, priming and triggering of membrane fusion/exocytosis) in DCV secretion.

Publication types

  • Review

MeSH terms

  • Animals
  • Catecholamines / metabolism
  • Chromaffin Cells / metabolism*
  • Exocytosis / physiology*
  • Humans
  • Peptides / metabolism
  • Secretory Vesicles / physiology*

Substances

  • Catecholamines
  • Peptides