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          Document History for Document ID 16643

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Document Version Version Comment Date Status
16643.0 [No comment] 20.09.2010 14:19 Released

ID: 16643.0, MPI für biophysikalische Chemie / Neurobiologie (Prof. Reinhard Jahn)
SNAREs in native plasma membranes are active and readily form core complexes with endogenous and exogenous SNAREs
Authors:Lang, T.; Margittai, M.; Hoelzler, H.; Jahn, R.
Language:English
Date of Publication (YYYY-MM-DD):2002-08-19
Title of Journal:Journal of Cell Biology
Volume:158
Issue / Number:4
Start Page:751
End Page:760
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:During neuronal exocytosis, the vesicle-bound soluble NSF attachment protein (SNAP) receptor (SNARE) synaptobrevin 2 forms complexes with the plasma membrane-bound SNAREs syntaxin 1A and SNAP25 to initiate the fusion reaction. However, it is not known whether in the native membrane SNAREs are constitutively active or whether they are unable to enter SNARE complexes unless activated before membrane fusion. Here we used binding of labeled recombinant SNAREs to inside-out carrier supported plasma membrane sheets of PC12 cells to probe for the activity of endogenous SNAREs. Binding was specific, saturable, and depended on the presence of membrane-resident SNARE partners. Our data show that virtually all of the endogenous syntaxin I and SNAP-25 are highly reactive and readily form SNARE complexes with exogenously added SNAREs. Furthermore, complexes between endogenous SNAREs were not detectable when the membranes are freshly prepared, but they slowly form upon prolonged incubation in vitro. We conclude that the activity of membrane-resident SNAREs is not downregulated by control proteins but is constitutively active even if not engaged in fusion events.
Free Keywords:exocytosis; membrane fusion; PC12 cells; in vitro; SNARE reactivity
Comment of the Author/Creator:Date: 2002, AUG 19
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Reinhard Jahn / 190/AG Thorsten Lang
MPI für biophysikalische Chemie/Abt. Stefan Hell / 200
Identifiers:URL:http://jcb.rupress.org/content/158/4/751.full.pdf+...