Docking and fusion in neurosecretion

被引:71
作者
Robinson, LJ [1 ]
Martin, TFJ [1 ]
机构
[1] Univ Wisconsin, Dept Biochem, Madison, WI 53706 USA
关键词
D O I
10.1016/S0955-0674(98)80063-X
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
A central issue in neurobiology concerns the mechanisms of membrane fusion that are essential for the rapid regulated delivery of neurotransmitters into the synapse. While many gene products are required for neurosecretion, recent research has focused on defining the core exocytotic machinery that is responsible for the docking of synaptic vesicles (SVs) and their fusion with the plasma membrane. N-ethylmaleimide-sensitive factor (NSF), soluble NSF attachment protein (SNAP) and SNAP receptor (SNARE) proteins are essential for fusion but may not be critical for SV docking. Current evidence suggests that NSF functions during an ATP-dependent step after docking but before fusion. NSF may function to liberate SNARE proteins from complexes so that the proteins on apposed membranes align in a parallel fashion to bring SVs into close contact with the plasma membrane for fusion.
引用
收藏
页码:483 / 492
页数:10
相关论文
共 73 条
[71]   A NOVEL 115-KD PERIPHERAL MEMBRANE-PROTEIN IS REQUIRED FOR INTERCISTERNAL TRANSPORT IN THE GOLGI STACK [J].
WATERS, MG ;
CLARY, DO ;
ROTHMAN, JE .
JOURNAL OF CELL BIOLOGY, 1992, 118 (05) :1015-1026
[72]   SNAREpins: Minimal machinery for membrane fusion [J].
Weber, T ;
Zemelman, BV ;
McNew, JA ;
Westermann, B ;
Gmachl, M ;
Parlati, F ;
Sollner, TH ;
Rothman, JE .
CELL, 1998, 92 (06) :759-772
[73]   LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion [J].
Xu, ZY ;
Sato, K ;
Wickner, W .
CELL, 1998, 93 (07) :1125-1134