ArticleThe Journal of cell biology1997
Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 177 citations in OpenAlex.
- A pathogenic mutation in α-SNAP impairs membrane lipid binding by concealing a critical hydrophobic loop.Communications biology · 2026Article
- Functional assembly of the Qc-SNARE with Sec18 and Sec17 on membranes.Molecular biology of the cell · 2026Article
- Evolutionary duplication of the leishmanial adaptor protein α-SNAP plays a role in its pathogenicity.The Journal of biological chemistry · 2025Article
- NSF/αSNAP2-mediated cis-SNARE complex disassembly precedes vesicle fusion in Arabidopsis cytokinesis.Nature plants · 2023Article
- PI3P regulates multiple stages of membrane fusion.Molecular biology of the cell · 2023Article
- Alpha-SNAP (M105I) mutation promotes neuronal differentiation of neural stem/progenitor cells through overactivation of AMPK.Frontiers in cell and developmental biology · 2023Article
- Sec18 supports membrane fusion by promoting Sec17 membrane association.Molecular biology of the cell · 2022Article
- Detection of rare nematode resistance Rhg1 haplotypes in Glycine soja and a novel Rhg1 α-SNAP.The plant genome · 2022Article
- Sec17/Sec18 can support membrane fusion without help from completion of SNARE zippering.eLife · 2021Article
- SNARE Regulatory Proteins in Synaptic Vesicle Fusion and Recycling.Frontiers in molecular neuroscience · 2021Review
- AtNSF regulates leaf serration by modulating intracellular trafficking of PIN1 in Arabidopsis thaliana.Journal of integrative plant biology · 2020Article
- The Intrinsically Disordered N-terminal Extension of the ClpS Adaptor Reprograms Its Partner AAA+ ClpAP Protease.Journal of molecular biology · 2020Article
- Zipcode RNA-Binding Proteins and Membrane Trafficking Proteins Cooperate to Transport Glutelin mRNAs in Rice Endosperm.The Plant cell · 2020Article
- The inner workings of intracellular heterotypic and homotypic membrane fusion mechanisms.Journal of biosciences · 2019Article
- Article
- 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
- Agnoprotein Is an Essential Egress Factor during BK Polyomavirus Infection.International journal of molecular sciences · 2018Article
- Assembly of intermediates for rapid membrane fusion.The Journal of biological chemistry · 2018Article
- Probing and manipulating intracellular membrane traffic by microinjection of artificial vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-ethylmaleimide-sensitive fusion protein (NSF) and alpha-SNAP play key roles in vesicular traffic through the secretory pathway. In this study, NH2- and COOH-terminal truncation mutants of alpha-SNAP were assayed for ability to bind NSF and stimulate its ATPase activity. Deletion of up to 160 NH2-terminal amino acids had little effect on the ability of alpha-SNAP to stimulate the ATPase activity of NSF. However, deletion of as few as 10 COOH-terminal amino acids resulted in a marked decrease. Both NH2-terminal (1-160) and COOH-terminal (160-295) fragments of alpha-SNAP were able to bind to NSF, suggesting that alpha-SNAP contains distinct NH2- and COOH-terminal binding sites for NSF. Sequence alignment of known SNAPs revealed only leucine 294 to be conserved in the final 10 amino acids of alpha-SNAP. Mutation of leucine 294 to alanine (alpha-SNAP(L294A)) resulted in a decrease in the ability to stimulate NSF ATPase activity but had no effect on the ability of this mutant to bind NSF. alpha-SNAP (1-285) and alpha-SNAP (L294A) were unable to stimulate Ca2+-dependent exocytosis in permeabilized chromaffin cells. In addition, alpha-SNAP (1-285), and alpha-SNAP (L294A) were able to inhibit the stimulation of exocytosis by exogenous alpha-SNAP. alpha-SNAP, alpha-SNAP (1-285), and alpha-SNAP (L294A) were all able to become incorporated into a 20S complex and recruit NSF. In the presence of MgATP, alpha-SNAP (1-285) and alpha-SNAP (L294A) were unable to fully disassemble the 20S complex and did not allow vesicle-associated membrane protein dissociation to any greater level than seen in control incubations. These findings imply that alpha-SNAP stimulation of NSF ATPase activity may be required for 20S complex disassembly and for the alpha-SNAP stimulation of exocytosis.
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