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

Robert D. Burgoyne, Alan Morgan

Open publisher page 102 citations

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.

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What this paper is about

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.

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Available 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.

Key concepts: Exocytosis, Munc-18, Cell biology, Biology, Chromaffin cell, Fusion protein, Lipid bilayer fusion, Function (biology)

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