Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
SNARE-complex disassembly by NSF follows synaptic-vesicle fusion
Autore:
Littleton, JT; Barnard, RJO; Titus, SA; Slind, J; Chapman, ER; Ganetzky, B;
Indirizzi:
MIT, Ctr Learing & Memory, Cambridge, MA 02139 USA MIT Cambridge MA USA 02139 Ctr Learing & Memory, Cambridge, MA 02139 USA Univ Wisconsin, Genet Lab, Madison, WI 53706 USA Univ Wisconsin Madison WI USA 53706 sin, Genet Lab, Madison, WI 53706 USA Univ Wisconsin, Dept Physiol, Madison, WI 53706 USA Univ Wisconsin Madison WI USA 53706 , Dept Physiol, Madison, WI 53706 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 21, volume: 98, anno: 2001,
pagine: 12233 - 12238
SICI:
0027-8424(20011009)98:21<12233:SDBNFS>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRYSTAL-STRUCTURE; NEUROTRANSMITTER RELEASE; VESICULAR TRANSPORT; TERMINAL DOMAIN; MEMBRANE-FUSION; ALPHA-SNAP; PROTEIN NSF; EXOCYTOSIS; DROSOPHILA; ATPASE;
Keywords:
neurotransmitter release; exocytosis; synapse; Drosophila;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Littleton, JT MIT, Ctr Learing & Memory, 50 Ames St,E18-672, Cambridge, MA02139 USA MIT 50 Ames St,E18-672 Cambridge MA USA 02139 , MA 02139 USA
Citazione:
J.T. Littleton et al., "SNARE-complex disassembly by NSF follows synaptic-vesicle fusion", P NAS US, 98(21), 2001, pp. 12233-12238

Abstract

Soluble N-ethylmaleimide-sensitive fusion attachment protein receptor (SNARE)-mediated fusion of synaptic vesicles with the presynaptic-plasma membrane is essential for communication between neurons. Disassembly of the SNAREcomplex requires the ATPase N-ethylmaleimide-sensitive fusion protein (NSF). To determine where in the synaptic-vesicle cycle NSF functions, we have undertaken a genetic analysis of comatose (dNSF-1) in Drosophila. Characterization of 16 comatose mutations demonstrates that NSF mediates disassemblyof SNARE complexes after synaptic-vesicle fusion. Hypomorphic mutations inNSF cause temperature-sensitive paralysis, whereas null mutations result in lethality. Genetic-interaction studies with para demonstrate that blocking evoked fusion delays the accumulation of assembled SNARE complexes and behavioral paralysis that normally occurs in comatose mutants, indicating NSFactivity is not required in the absence of vesicle fusion. In addition, the entire vesicle pool can be depleted in shibire comatose double mutants, demonstrating that NSF activity is not required for the fusion step itself. Multiple rounds of vesicle fusion in the absence of NSF activity poisons neurotransmission by trapping SNAREs into cis-complexes. These data indicate that NSF normally dissociates and recycles SNARE proteins during the interval between exocytosis and endocytosis. In the absence of NSF activity, there are sufficient fusion-competent SNAREs to exocy-tose both the readily released and the reserve pool of synaptic vesicles.ceptor (SNARE)-mediated fusion of synaptic vesicles with the presynaptic-plasma membrane is essential for communication between neurons. Disassembly of the SNARE complex requires the ATPase N-ethylmaleimide-sensitive fusion protein (NSF). To determine where in the synaptic-vesicle cycle NSF functions, we have undertaken a genetic analysis of comatose (dNSF-1) in Drosophila. Characterization of 16 comatose mutations demonstrates that NSF mediates disassembly of SNARE complexes after synaptic-vesicle fusion. Hypomorphic mutations in NSF cause temperature-sensitive paralysis, whereas null mutations result in lethality. Genetic-interaction studies with para demonstrate that blocking evoked fusion delays the accumulation of assembled SNARE complexes and behavioral paralysis that normally occurs in comatose mutants, indicating NSF activity is notrequired in the absence of vesicle fusion. In addition, the entire vesiclepool can be depleted in shibire comatose double mutants, demonstrating that NSF activity is not required for the fusion step itself. Multiple rounds of vesicle fusion in the absence of NSF activity poisons neurotransmission by trapping SNAREs into cis-complexes. These data indicate that NSF normally dissociates and recycles SNARE proteins during the interval between exocytosis and endocytosis. In the absence of NSF activity, there are sufficientfusion-competent SNAREs to exocy-tose both the readily released and the reserve pool of synaptic vesicles.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/01/21 alle ore 22:48:22