ArticleMolecular biology of the cell1996
Domains of alpha-SNAP required for the stimulation of exocytosis and for N-ethylmalemide-sensitive fusion protein (NSF) binding and activation.
Article in Molecular biology of the cell, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 57 citations in OpenAlex.
- Functional assembly of the Qc-SNARE with Sec18 and Sec17 on membranes.Molecular biology of the cell · 2026Article
- Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025Article
- Evolutionary duplication of the leishmanial adaptor protein α-SNAP plays a role in its pathogenicity.The Journal of biological chemistry · 2025Article
- The role of synaptic protein NSF in the development and progression of neurological diseases.Frontiers in neuroscience · 2024Review
- PI3P regulates multiple stages of membrane fusion.Molecular biology of the cell · 2023Article
- Sec18 supports membrane fusion by promoting Sec17 membrane association.Molecular biology of the cell · 2022Article
- An atypical N-ethylmaleimide sensitive factor enables the viability of nematode-resistantProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Sec17 (α-SNAP) and an SM-tethering complex regulate the outcome of SNARE zippering in vitro and in vivo.eLife · 2017Article
- The soybean GmSNAP18 gene underlies two types of resistance to soybean cyst nematode.Nature communications · 2017Article
- Disease resistance through impairment of α-SNAP-NSF interaction and vesicular trafficking by soybean Rhg1.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Cryo-EM structure of SNAP-SNARE assembly in 20S particle.Cell research · 2015Article
- Article
- Distinct Copy Number, Coding Sequence, and Locus Methylation Patterns Underlie Rhg1-Mediated Soybean Resistance to Soybean Cyst Nematode.Plant physiology · 2014Article
- The expression of a naturally occurring, truncated allele of an α-SNAP gene suppresses plant parasitic nematode infection.Plant molecular biology · 2012Article
- Nucleotide-dependent conformational changes in the N-Ethylmaleimide Sensitive Factor (NSF) and their potential role in SNARE complex disassembly.Journal of structural biology · 2012Article
- Requirements for the catalytic cycle of the N-ethylmaleimide-Sensitive Factor (NSF).Biochimica et biophysica acta · 2012Review
- Time-course investigation of SAGM-stored leukocyte-filtered red bood cell concentrates: from metabolism to proteomics.Haematologica · 2012Article
- α-SNAP prevents docking of the acrosome during sperm exocytosis because it sequesters monomeric syntaxin.PloS one · 2011Article
- Dissecting the N-ethylmaleimide-sensitive factor: required elements of the N and D1 domains.The Journal of biological chemistry · 2010Article
- Sorting in early endosomes reveals connections to docking- and fusion-associated factors.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The binding of alpha-SNAP to the membrane proteins syntaxin, SNAP-25, and synaptobrevin leads to the recruitment of the N-ethylmaleimide-sensitive fusion protein (NSF). ATP hydrolysis by NSF has been suggested to drive conformational changes in one or more of these membrane proteins that are essential for regulated exocytosis. Functional evidence for a role of alpha-SNAP in exocytosis in adrenal chromaffin cells comes from the ability of this protein to stimulate Ca(2+)-dependent exocytosis in digitonin-permeabilized cells. Here we examine the effect of a series of deletion mutants of alpha-SNAP on exocytosis, and on the ability of alpha-SNAP to interact with NSF, to define essential domains involved in protein-protein interactions in exocytosis. Deletion of extreme N- or C-terminal regions of alpha-SNAP produced proteins unable to bind to syntaxin or to stimulate exocytosis, suggesting that these domains participate in essential interactions. Deletion of C-terminal residues abolished the ability of alpha-SNAP to bind NSF. In contrast, deletion of up to 120 N-terminal residues did not prevent the binding of NSF to immobilized alpha-SNAP and such mutants were also able to stimulate the ATPase activity of NSF. These results suggest that the C-terminus, but not the N-terminus, of alpha-SNAP is crucial for interactions with NSF. The involvement of the C-terminus of alpha-SNAP, which contains a predicted coiled-coil domain, in the binding of both syntaxin and NSF would place the latter two proteins in proximity in a ternary complex whereupon the energy derived from ATP hydrolysis by NSF could induce a conformational change in syntaxin required for exocytosis to proceed.
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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.