ReviewBiochimica et biophysica acta2012
Requirements for the catalytic cycle of the N-ethylmaleimide-Sensitive Factor (NSF).
Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
42 citing papers in PubMed, 59 citations in OpenAlex.
- Article
- The role of synaptic protein NSF in the development and progression of neurological diseases.Frontiers in neuroscience · 2024Review
- Endothelial Cell-Pericyte Interactions in the Pathogenesis of Cerebral Cavernous Malformations (CCMs).Cold Spring Harbor perspectives in medicine · 2023Review
- Consecutive functions of small GTPases guide HOPS-mediated tethering of late endosomes and lysosomes.Cell reports · 2023Article
- Membrane protein trafficking in the anti-tumor immune response: work of endosomal-lysosomal system.Cancer cell international · 2022Review
- Tau target identification reveals NSF-dependent effects on AMPA receptor trafficking and memory formation.The EMBO journal · 2022Article
- The manifold roles of protein S-nitrosylation in the life of insulin.Nature reviews. Endocrinology · 2022Review
- Extreme parsimony in ATP consumption by 20S complexes in the global disassembly of single SNARE complexes.Nature communications · 2021Article
- AtNSF regulates leaf serration by modulating intracellular trafficking of PIN1 in Arabidopsis thaliana.Journal of integrative plant biology · 2020Article
- Copper Supplementation, A Challenge in Cattle.Animals : an open access journal from MDPI · 2020Review
- A Mechanistic Perspective on PEX1 and PEX6, Two AAA+ Proteins of the Peroxisomal Protein Import Machinery.International journal of molecular sciences · 2019Review
- Mechanistic insights into the SNARE complex disassembly.Science advances · 2019Article
- Cytokine exocytosis and JAK/STAT activation in theJournal of cell science · 2018Article
- Roles of Cellular NSF Protein in Entry and Nuclear Egress of Budded Virions of Autographa californica Multiple Nucleopolyhedrovirus.Journal of virology · 2017Article
- The nuts and bolts of the platelet release reaction.Platelets · 2017Review
- Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.Frontiers in molecular biosciences · 2017Review
- Dopamine D1A directly interacts with otoferlin synaptic pathway proteins: Ca2+ and phosphorylation underlie an NSF-to-AP2mu1 molecular switch.The Biochemical journal · 2017Article
- Shedding light on the expansion and diversification of the Cdc48 protein family during the rise of the eukaryotic cell.BMC evolutionary biology · 2016Article
- Structures of the double-ring AAA ATPase Pex1-Pex6 involved in peroxisome biogenesis.The FEBS journal · 2016Review
- Oxaspirol B with p97 Inhibitory Activity and Other Oxaspirols from Lecythophora sp. FL1375 and FL1031, Endolichenic Fungi Inhabiting Parmotrema tinctorum and Cladonia evansii.Journal of natural products · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The N-ethylmaleimide-Sensitive Factor (NSF) was one of the initial members of the ATPases Associated with various cellular Activities Plus (AAA(+)) family. In this review, we discuss what is known about the mechanism of NSF action and how that relates to the mechanisms of other AAA(+) proteins. Like other family members, NSF binds to a protein complex (i.e., SNAP-SNARE complex) and utilizes ATP hydrolysis to affect the conformations of that complex. SNAP-SNARE complex disassembly is essential for SNARE recycling and sustained membrane trafficking. NSF is a homo-hexamer; each protomer is composed of an N-terminal domain, NSF-N, and two adjacent AAA-domains, NSF-D1 and NSF-D2. Mutagenesis analysis has established specific roles for many of the structural elements of NSF-D1, the catalytic ATPase domain, and NSF-N, the SNAP-SNARE binding domain. Hydrodynamic analysis of NSF, labeled with (Ni(2+)-NTA)(2)-Cy3, detected conformational differences in NSF, in which the ATP-bound conformation appears more compact than the ADP-bound form. This indicates that NSF undergoes significant conformational changes as it progresses through its ATP-hydrolysis cycle. Incorporating these data, we propose a sequential mechanism by which NSF uses NSF-N and NSF-D1 to disassemble SNAP-SNARE complexes. We also illustrate how analytical centrifugation might be used to study other AAA(+) proteins.
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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.