ArticleMolecular biology of the cell2008
The structural and functional implications of linked SNARE motifs in SNAP25.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
- Munc18 reprograms the intrinsic neuronal SNARE complex assembly pathway.bioRxiv : the preprint server for biology · 2026Article
- Multiple structural states in an intrinsically disordered protein, SNAP-25, using circular dichroism.Biophysical journal · 2025Article
- Functionally distinct SNARE motifs of SNAP25 cooperate in SNARE assembly and membrane fusion.Biophysical journal · 2025Article
- VAMP2 and synaptotagmin mobility in chromaffin granule membranes: implications for regulated exocytosis.Molecular biology of the cell · 2022Article
- Roles for the SNAP25 linker domain in the fusion pore and a dynamic plasma membrane SNARE "acceptor" complex.The Journal of general physiology · 2020Article
- Regulatory Mechanism of SNAP23 in Phagosome Formation and Maturation.Yonago acta medica · 2020Review
- Article
- GhSNAP33, a t-SNARE Protein FromFrontiers in plant science · 2018Article
- The influence of cell membrane and SNAP25 linker loop on the dynamics and unzipping of SNARE complex.PloS one · 2017Article
- How could SNARE proteins open a fusion pore?Physiology (Bethesda, Md.) · 2014Review
- Rapid structural change in synaptosomal-associated protein 25 (SNAP25) precedes the fusion of single vesicles with the plasma membrane in live chromaffin cells.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Single cell optical imaging and spectroscopy.Chemical reviews · 2013Review
- SNAP-23 regulates phagosome formation and maturation in macrophages.Molecular biology of the cell · 2012Article
- SNARE requirements en route to exocytosis: from many to few.Journal of molecular neuroscience : MN · 2012Review
- A new role for the dynamin GTPase in the regulation of fusion pore expansion.Molecular biology of the cell · 2011Article
- Imaging with total internal reflection fluorescence microscopy for the cell biologist.Journal of cell science · 2010Review
- The t-SNARE complex: a close up.Cellular and molecular neurobiology · 2010Review
- Systems microscopy approaches to understand cancer cell migration and metastasis.Cellular and molecular life sciences : CMLS · 2010Review
- Chemomechanical regulation of SNARE proteins studied with molecular dynamics simulations.Biophysical journal · 2010Article
- Calmodulin is a functional regulator of Cav1.4 L-type Ca2+ channels.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We investigated the functional and structural implications of SNAP25 having two SNARE motifs (SN1 and SN2). A membrane-bound, intramolecular FRET probe was constructed to report on the folding of N-terminal SN1 and C-terminal SN2 in living cells. Membrane-bound constructs containing either or both SNARE motifs were also singly labeled with donor or acceptor fluorophores. Interaction of probes with other SNAREs was monitored by the formation of SDS-resistant complexes and by changes in FRET measured in vitro using spectroscopy and in the plasma membrane of living cells using TIRF microscopy. The probes formed the predicted SDS-resistant SNARE complexes. FRET measurements revealed that syntaxin induced a close association of the N-termini of SN1 and SN2. This association required that the SNARE motifs reside in the same molecule. Unexpectedly, the syntaxin-induced FRET was prevented by VAMP. Both full-length SNAP25 constructs and the combination of its separated, membrane-bound constituent chains supported secretion in permeabilized chromaffin cells that had been allowed to rundown. However, only full-length SNAP25 constructs enabled robust secretion from intact cells or permeabilized cells before rundown. The experiments suggest that the bidentate structure permits specific conformations in complexes with syntaxin and VAMP and facilitates the function of SN1 and SN2 in exocytosis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.