ArticleThe EMBO journal2000
Putative fusogenic activity of NSF is restricted to a lipid mixture whose coalescence is also triggered by other factors.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 32 citations in OpenAlex.
- Article
- Article
- The final conformation of the complete ectodomain of the HA2 subunit of influenza hemagglutinin can by itself drive low pH-dependent fusion.The Journal of biological chemistry · 2011Article
- Transmembrane protein-free membranes fuse into xenopus nuclear envelope and promote assembly of functional pores.The Journal of biological chemistry · 2009Article
- Phosphatidylinositol 4,5-bisphosphate regulates SNARE-dependent membrane fusion.The Journal of cell biology · 2008Article
- A novel site of action for alpha-SNAP in the SNARE conformational cycle controlling membrane fusion.Molecular biology of the cell · 2008Article
- Transmembrane proteins are not required for early stages of nuclear envelope assembly.The Biochemical journal · 2006Article
- A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion.The EMBO journal · 2004Article
- Ganglioside glycosyltransferases and newly synthesized gangliosides are excluded from detergent-insoluble complexes of Golgi membranes.The Biochemical journal · 2004Article
- Sequential SNARE disassembly and GATE-16-GOS-28 complex assembly mediated by distinct NSF activities drives Golgi membrane fusion.The Journal of cell biology · 2002Article
- Yeast vacuoles and membrane fusion pathways.The EMBO journal · 2002Review
- SNAREpins are functionally resistant to disruption by NSF and alphaSNAP.The Journal of cell biology · 2000Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has recently been reported that N-ethylmaleimide-sensitive fusion ATPase (NSF) can fuse protein-free liposomes containing substantial amounts of 1,2-dioleoylphosphatidylserine (DOPS) and 1, 2-dioleoyl-phosphatidyl-ethanolamine (DOPE) (Otter-Nilsson et al., 1999). The authors impart physiological significance to this observation and propose to re-conceptualize the general role of NSF in fusion processes. We can confirm that isolated NSF can fuse liposomes of the specified composition. However, this activity of NSF is resistant to inactivation by N-ethylmaleimide and does not depend on the presence of alpha-SNAP (soluble NSF-attachment protein). Moreover, under the same conditions, either alpha-SNAP, other proteins apparently unrelated to vesicular transport (glyceraldehyde-3-phosphate dehydrogenase or lactic dehydrogenase) or even 3 mM magnesium ions can also cause lipid mixing. In contrast, neither NSF nor the other proteins nor magnesium had any significant fusogenic activity with liposomes composed of a biologically occurring mixture of lipids. A straightforward explanation is that the lipid composition chosen as optimal for NSF favors non-specific fusion because it is physically unstable when formed into liposomes. A variety of minor perturbations could then trigger coalescence.
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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.