TY - JOUR
T1 - Distinct domains of syntaxin are required for synaptic vesicle fusion complex formation and dissociation
AU - Kee, Yun
AU - Lin, Richard C.
AU - Hsu, Shu Chan
AU - Scheller, Richard H.
N1 - Funding Information:
We thank Dr. Tony Ting for helpful comments on this manuscript and Dr. Mark Bennett for syntaxin deletion mutant constructs. This work is supported by the National Institute of Mental Health. R. C. L. is a Medical Scientist Training Program trainee funded by the National Institute of General Medical Sciences. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 USC Section 1734 solely to indicate this fact.
PY - 1995/5
Y1 - 1995/5
N2 - Membrane fusion resulting in neurotransmitter secretion forms the basis of neural communication. Three multimeric complexes of the protein syntaxin are important in this process: syntaxin and n-sect; syntaxin, VAMP, and SNAP-25; and syntaxin, VAMP, SNAP-25, αSNAP, and NSF (20S complex). In this report, we demonstrate that unique, yet overlapping, domains of syntaxin are required to form these complexes. The formation of higher order heteromultimers has a set of structural requirements distinct from those required for dimeric interactions. Dissociation of the 20S complex by NSF following ATP hydrolysis requires aminoterminal regions of syntaxin that are outside of the binding domains for the 20S constituent proteins. These data are consistent with the hypothesis that conformational changes in syntaxin, resulting from protein-protein interactions and ATP hydrolysis by NSF, mediate neurotransmitter release.
AB - Membrane fusion resulting in neurotransmitter secretion forms the basis of neural communication. Three multimeric complexes of the protein syntaxin are important in this process: syntaxin and n-sect; syntaxin, VAMP, and SNAP-25; and syntaxin, VAMP, SNAP-25, αSNAP, and NSF (20S complex). In this report, we demonstrate that unique, yet overlapping, domains of syntaxin are required to form these complexes. The formation of higher order heteromultimers has a set of structural requirements distinct from those required for dimeric interactions. Dissociation of the 20S complex by NSF following ATP hydrolysis requires aminoterminal regions of syntaxin that are outside of the binding domains for the 20S constituent proteins. These data are consistent with the hypothesis that conformational changes in syntaxin, resulting from protein-protein interactions and ATP hydrolysis by NSF, mediate neurotransmitter release.
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U2 - 10.1016/0896-6273(95)90337-2
DO - 10.1016/0896-6273(95)90337-2
M3 - Article
C2 - 7748566
AN - SCOPUS:0029058496
SN - 0896-6273
VL - 14
SP - 991
EP - 998
JO - Neuron
JF - Neuron
IS - 5
ER -