Abstract
N-Ethylmaleimide-sensitive factor (NSF) is required for multiple pathways of vesicle-mediated protein transport. Microinjection of a monoclonal anti-NSF antibody almost completely blocked brefeldin A-promoted Golgi disassembly without affecting the rapid release of beta-COP, a subunit of the Golgi coat proteins (COPI), from the Golgi apparatus. Similar results were obtained using a dominant-negative NSF which is known to compete with endogenous NSF. The present results suggest that an NSF-mediated step is present in the brefeldin A-promoted disassembly of the Golgi apparatus.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Anti-Bacterial Agents / pharmacology
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Brefeldin A
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CHO Cells
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Carrier Proteins / metabolism*
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Cricetinae
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Cyclopentanes / pharmacology*
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Golgi Apparatus / drug effects
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Golgi Apparatus / metabolism*
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Golgi Apparatus / ultrastructure*
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Macrolides
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Microscopy, Electron
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N-Ethylmaleimide-Sensitive Proteins
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Protein Synthesis Inhibitors / pharmacology*
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Vesicular Transport Proteins*
Substances
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Anti-Bacterial Agents
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Carrier Proteins
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Cyclopentanes
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Macrolides
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Protein Synthesis Inhibitors
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Vesicular Transport Proteins
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Brefeldin A
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N-Ethylmaleimide-Sensitive Proteins