Author: | Söllner, T. H. |
Article Title: | Regulated exocytosis and SNARE function |
Abstract: | The pairing of cognate v- and t-SNAREs between two opposing lipid bilayers drives spontaneous membrane fusion and confers specificity to intracellular membrane trafficking. These fusion events are regulated by a cascade of protein-protein interactions that locally control SNARE activity and complex assembly, determining when and where fusion occurs with high efficiency in vivo. This basic regulation occurs at all transport steps and is mediated by conserved protein families such as Rab proteins and their effectors and Sec1/unc18 proteins. Regulated exocytosis employs auxiliary components that couple the signal (which triggers exocytosis) to the fusion machinery. At the neuronal synapse, munc13 as well as munc18 control SNARE complex assembly. Synaptotagmin and complexin ensure fast synchronous calcium-evoked neurotransmitter release. |
Keywords: | signal transduction; unclassified drug; review; animals; complex formation; protein protein interaction; cell protein; membrane proteins; calcium; regulatory mechanism; carrier proteins; cell membrane; effector cell; protein family; nerve cell; membrane transport; lipid bilayer; synaptotagmin; exocytosis; fusion; synapse; vesicular transport proteins; neurotransmission; membrane biology; membrane fusion; neurotransmitter release; vesicle; snare protein; neurotransmitter; rab protein; snare proteins; snare; humans; priority journal; nsf; protein sec1; n-ethylmaleimide-sensitive proteins; soluble n-ethylmaleimide-sensitive factor attachment proteins |
Journal Title: | Molecular Membrane Biology |
Volume: | 20 |
Issue: | 3 |
ISSN: | 0968-7688 |
Publisher: | Informa Healthcare |
Date Published: | 2003-07-01 |
Start Page: | 209 |
End Page: | 220 |
Language: | English |
DOI: | 10.1080/0968768031000104953 |
PUBMED: | 12893529 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | Export Date: 25 September 2014 -- Source: Scopus |