NSF is required for the brefeldin A‐promoted disassembly of the Golgi apparatus
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Summary
The present results suggest that an NSF‐mediated step is present in the brefeldin A‐promoted disassembly of the Golgi apparatus.
- Type
- article
- Published
- 1998-09-18
- Cited by
- 15
- References
- 37
- OpenAlex
- https://openalex.org/W2093614800
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:21628432
Keywords
Brefeldin A, Golgi apparatus, COPI, Microinjection, Cell biology
References
- Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF
- Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic.
- Role of two nucleotide-binding regions in an N-ethylmaleimide-sensitive factor involved in vesicle-mediated protein transport.
- Binding of coatomer to Golgi membranes requires ADP-ribosylation factor.
- Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport.
- Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum.
- The formation of Golgi stacks from vesiculated Golgi membranes requires two distinct fusion events.
- A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion.
- Stages of regulated exocytosis.
- A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast
- Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action
- SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast.
- ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes.
- Diffusional Mobility of Golgi Proteins in Membranes of Living Cells
- Golgi Tubule Traffic and the Effects of Brefeldin A Visualized in Living Cells
- Selective inhibition of transcytosis by brefeldin A in MDCK cells.
- Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein
- A role for calmodulin in organelle membrane tubulation.
- A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein β-adaptin
- Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy.
Cited by
- N-ethylmaleimide sensitive factor (NSF) structure and function.
- Implication of ZW10 in membrane trafficking between the endoplasmic reticulum and Golgi
- Biochemical Mechanisms of the Generation of Endogenous Long Chain Ceramide in Response to Exogenous Short Chain Ceramide in the A549 Human Lung Adenocarcinoma Cell Line
- The AAA-ATPase NVL2 is a component of pre-ribosomal particles that interacts with the DExD/H-box RNA helicase DOB1.
- Mechanism of constitutive export from the golgi: bulk flow via the formation, protrusion, and en bloc cleavage of large trans-golgi network tubular domains.
- ER-to-Golgi carriers arise through direct en bloc protrusion and multistage maturation of specialized ER exit domains.
- Reconstitution of brefeldin A-induced golgi tubulation and fusion with the endoplasmic reticulum in semi-intact chinese hamster ovary cells.
- Implication of sphingolipid metabolism in the stability of the Golgi apparatus.
- Cell surface membrane homeostasis and intracellular membrane traffic balance in mouse L929 cells.
- Dopamine reduces cell surface Na+/H+ exchanger-3 protein by decreasing NHE3 exocytosis and cell membrane recycling.
- Models of Intracellular Transport: Pros and Cons
- Role of Intracellular Transport in the Centriole-Dependent Formation of Golgi Ribbon.
- Semi-Intact Cell System for Reconstituting and Analyzing Cellular Golgi Dynamics.
- Molecular Mechanism of Renal Tubule Transport Dopamine reduces cell surface Na (cid:2) /H (cid:2) exchanger-3 protein by decreasing NHE3 exocytosis and cell membrane recycling
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