Promiscuous interaction of SNAP-25 with all plasma membrane syntaxins in a neuroendocrine cell

被引:31
作者
Bajohrs, M [1 ]
Darios, F [1 ]
Peak-Chew, SY [1 ]
Davletov, B [1 ]
机构
[1] MRC, Mol Biol Lab, Cambridge CB2 2QH, England
关键词
chromaffin cell; PC12; cell; 25kDa synaptosome-associated protein (SNAP-25); soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE); syntaxin; tumour;
D O I
10.1042/BJ20050583
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
SNAP-25 (25 kDa synaptosome-associated protein) is found in cells that release neurotransmitters and hormones, and plays a central role in the fusion of secretory vesicles with the plasma membrane. SNAP-25 has been shown to interact specifically with syntaxin 1, a 35 kDa membrane protein, to mediate the fusion process. Here, we investigated whether other known syntaxin isoforms found at the plasma membrane can serve as binding partners for SNAP-25 in vivo. In our analysis, we employed rat phaeo-chromocytoma PC12 cells that are often used as a model of neuronal functions. We now show that these cells contain large amounts of SNAP-25, which interacts not only with syntaxin 1, but also with ubiquitous syntaxins 2, 3 and 4. The plasma membrane syntaxins appear to Occupy complementary domains at the plasma membrane. In defined reactions, the ubiquitous plasma membrane syntaxin isoforms, when in binary complexes with SNAP-25, readily bound vesicular synaptobrevin to form SDS-resistant SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) complexes implicated in membrane fusion. However, vesicular synaptotagmin and cytosolic complexin, both implicated in the fusion process, exhibited differential ability to interact with the SNARE complexes formed by syntaxins 1-4, suggesting that file plasma membrane syntaxins may mediate vesicle fusion events with different properties.
引用
收藏
页码:283 / 289
页数:7
相关论文
共 46 条
[1]   Complexin regulates the closure of the fusion pore during regulated vesicle exocytosis [J].
Archer, DA ;
Graham, ME ;
Burgoyne, RD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (21) :18249-18252
[2]   A molecular basis underlying differences in the toxicity of botulinum serotypes A and E [J].
Bajohrs, M ;
Rickman, C ;
Binz, T ;
Davletov, B .
EMBO REPORTS, 2004, 5 (11) :1090-1095
[3]   THE SYNTAXIN FAMILY OF VESICULAR TRANSPORT RECEPTORS [J].
BENNETT, MK ;
GARCIAARRARAS, JE ;
ELFERINK, LA ;
PETERSON, K ;
FLEMING, AM ;
HAZUKA, CD ;
SCHELLER, RH .
CELL, 1993, 74 (05) :863-873
[4]   A genomic perspective on membrane compartment organization [J].
Bock, JB ;
Matern, HT ;
Peden, AA ;
Scheller, RH .
NATURE, 2001, 409 (6822) :839-841
[5]   Secretory granule exocytosis [J].
Burgoyne, RD ;
Morgan, A .
PHYSIOLOGICAL REVIEWS, 2003, 83 (02) :581-632
[6]   Mixed and non-cognate SNARE complexes - Characterization of assembly and biophysical properties [J].
Fasshauer, D ;
Antonin, W ;
Margittai, M ;
Pabst, S ;
Jahn, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (22) :15440-15446
[7]   A structural change occurs upon binding of syntaxin to SNAP-25 [J].
Fasshauer, D ;
Bruns, D ;
Shen, B ;
Jahn, R ;
Brunger, AT .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (07) :4582-4590
[8]   A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells [J].
Galli, T ;
Zahraoui, A ;
Vaidyanathan, VV ;
Raposo, G ;
Tian, JM ;
Karin, M ;
Niemann, H ;
Louvard, D .
MOLECULAR BIOLOGY OF THE CELL, 1998, 9 (06) :1437-1448
[9]   Glucose uptake in PC12 cells: GLUT3 vesicle trafficking and fusion as revealed with a novel GLUT3-GFP fusion protein [J].
Greenlee, MHW ;
Uemura, E ;
Carpenter, SL ;
Doyle, RT ;
Buss, JE .
JOURNAL OF NEUROSCIENCE RESEARCH, 2003, 73 (04) :518-525
[10]   Vesicular restriction of synaptobrevin suggests a role for calcium in membrane fusion [J].
Hu, K ;
Carroll, J ;
Fedorovich, S ;
Rickman, C ;
Sukhodub, A ;
Davletov, B .
NATURE, 2002, 415 (6872) :646-650