Human Interaction Network Ontology

Last uploaded: June 27, 2014
Preferred Name

Proteolytic cleavage of SNARE complex proteins

Synonyms
Definitions

Authored: Krupa, S, Gopinathrao, G, 2006-06-15 10:36:11 VAMP/synaptobrevin, SNAP-25 and syntaxin are important for synaptic vesicle fusion at the nerve terminal. These proteins constitute the synaptic members of SNARE family (soluble N-ethylmaleimide-sensitive fusion protein) attachment protein receptor, which is central to all membrane fusion events (Umland et al. 1997). These proteins are involved in docking and/or fusion of synaptic vesicles with the presynaptic membrane. BoNTs achieve total blockage of neurotransmitter release by selectively inactivating the synaptic SNAREs by proteolysis.<br>The L chains of BoNTs of different serotypes specifically cleave distinct members of the SNARE family: serotypes B, D, F and G act on VAMP/synaptobrevin localized on synaptic vesicles; BoNT-A and E cleave SNAP-25; and BoNT-C cleaves both syntaxin 1 and SNAP-25, two proteins of the pre-synaptic plasma membrane.<br>Sudhof et al. (2001) and Liu et al. (2005) had observed that alpha-laterotoxins from black widow spider target identical neurmuscular junctions by opposite mechanism resulting in massive vesicle exocytosis. The exact molecular details of the action of these toxins may reveal the underlying processes of synaptic vesicle exocytosis/inbition and their regulation. Edited: Gopinathrao, G, 2006-06-15 22:12:29 Reviewed: Ichtchenko, K, 2007-08-03 18:17:25

ID

http://purl.obolibrary.org/obo/HINO_0015701

comment

Authored: Krupa, S, Gopinathrao, G, 2006-06-15 10:36:11

VAMP/synaptobrevin, SNAP-25 and syntaxin are important for synaptic vesicle fusion at the nerve terminal. These proteins constitute the synaptic members of SNARE family (soluble N-ethylmaleimide-sensitive fusion protein) attachment protein receptor, which is central to all membrane fusion events (Umland et al. 1997). These proteins are involved in docking and/or fusion of synaptic vesicles with the presynaptic membrane. BoNTs achieve total blockage of neurotransmitter release by selectively inactivating the synaptic SNAREs by proteolysis.
The L chains of BoNTs of different serotypes specifically cleave distinct members of the SNARE family: serotypes B, D, F and G act on VAMP/synaptobrevin localized on synaptic vesicles; BoNT-A and E cleave SNAP-25; and BoNT-C cleaves both syntaxin 1 and SNAP-25, two proteins of the pre-synaptic plasma membrane.
Sudhof et al. (2001) and Liu et al. (2005) had observed that alpha-laterotoxins from black widow spider target identical neurmuscular junctions by opposite mechanism resulting in massive vesicle exocytosis. The exact molecular details of the action of these toxins may reveal the underlying processes of synaptic vesicle exocytosis/inbition and their regulation.

Edited: Gopinathrao, G, 2006-06-15 22:12:29

Reviewed: Ichtchenko, K, 2007-08-03 18:17:25

definition source

Pubmed12417130

Pubmed16101679

Pubmed11520923

Reactome, http://www.reactome.org

Pubmed10865130

Pubmed9334741

Pubmed7527117

label

Proteolytic cleavage of SNARE complex proteins

located_in

http://purl.obolibrary.org/obo/NCBITaxon_9606

prefixIRI

HINO:0015701

prefLabel

Proteolytic cleavage of SNARE complex proteins

seeAlso

Reactome Database ID Release 43168782

ReactomeREACT_11242

subClassOf

http://purl.obolibrary.org/obo/INO_0000021

has_part

http://purl.obolibrary.org/obo/HINO_0015700

http://purl.obolibrary.org/obo/HINO_0015706

http://purl.obolibrary.org/obo/HINO_0026729

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http://scai.fraunhofer.de/PWDICT#ID1781 PTS LOOM