ArticleThe Journal of biological chemistry2010
Dissecting the N-ethylmaleimide-sensitive factor: required elements of the N and D1 domains.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 39 citations in OpenAlex.
- The role of synaptic protein NSF in the development and progression of neurological diseases.Frontiers in neuroscience · 2024Review
- mRNA Localization to the Endoplasmic Reticulum in Plant Endosperm Cells.International journal of molecular sciences · 2022Review
- Does GEC1 Enhance Expression and Forward Trafficking of the Kappa Opioid Receptor (KOR) via Its Ability to Interact with NSF Directly?Handbook of experimental pharmacology · 2022Article
- Zipcode RNA-Binding Proteins and Membrane Trafficking Proteins Cooperate to Transport Glutelin mRNAs in Rice Endosperm.The Plant cell · 2020Article
- 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
- 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
- The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading.Nature communications · 2018Article
- Allelic Expression Imbalance Promoting a Mutant PEX6 Allele Causes Zellweger Spectrum Disorder.American journal of human genetics · 2017Article
- Roles of Cellular NSF Protein in Entry and Nuclear Egress of Budded Virions of Autographa californica Multiple Nucleopolyhedrovirus.Journal of virology · 2017Article
- Recent Advances in Deciphering the Structure and Molecular Mechanism of the AAA+ ATPase N-Ethylmaleimide-Sensitive Factor (NSF).Journal of molecular biology · 2016Review
- Article
- Altered cofactor regulation with disease-associated p97/VCP mutations.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover.Science (New York, N.Y.) · 2015Article
- Article
- Structural mechanisms of chaperone mediated protein disaggregation.Frontiers in molecular biosciences · 2014Review
- Early consolidation of development and physiology of an identified presynaptic nerve terminal.BMC neuroscience · 2013Article
- Disassembly of all SNARE complexes by N-ethylmaleimide-sensitive factor (NSF) is initiated by a conserved 1:1 interaction between α-soluble NSF attachment protein (SNAP) and SNARE complex.The Journal of biological chemistry · 2013Article
- Processive ATP-driven substrate disassembly by the N-ethylmaleimide-sensitive factor (NSF) molecular machine.The Journal of biological chemistry · 2013Article
- Expanding proteostasis by membrane trafficking networks.Cold Spring Harbor perspectives in biology · 2013Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
N-Ethylmaleimide-sensitive factor (NSF) is a homo-hexameric member of the AAA(+) (ATPases associated with various cellular activities plus) family. It plays an essential role in most intracellular membrane trafficking through its binding to and disassembly of soluble NSF attachment protein (SNAP) receptor (SNARE) complexes. Each NSF protomer contains an N-terminal domain (NSF-N) and two AAA domains, a catalytic NSF-D1 and a structural NSF-D2. This study presents detailed mutagenesis analyses of NSF-N and NSF-D1, dissecting their roles in ATP hydrolysis, SNAP.SNARE binding, and complex disassembly. Our results show that a positively charged surface on NSF-N, bounded by Arg(67) and Lys(105), and the conserved residues in the central pore of NSF-D1 (Tyr(296) and Gly(298)) are involved in SNAP.SNARE binding but not basal ATP hydrolysis. Mutagenesis of Sensor 1 (Thr(373)-Arg(375)), Sensor 2 (Glu(440)-Glu(442)), and Arginine Fingers (Arg(385) and Arg(388)) in NSF-D1 shows that each region plays a discrete role. Sensor 1 is important for basal ATPase activity and nucleotide binding. Sensor 2 plays a role in ATP- and SNAP-dependent SNARE complex binding and disassembly but does so in cis and not through inter-protomer interactions. Arginine Fingers are important for SNAP.SNARE complex-stimulated ATPase activity and complex disassembly. Mutants at these residues have a dominant-negative phenotype in cells, suggesting that Arginine Fingers function in trans via inter-protomer interactions. Taken together, these data establish functional roles for many of the structural elements of the N domain and of the D1 ATP-binding site of NSF.
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