Molar mass 280.36 g/mol | ||
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Appearance White to off-white crystalline powder | ||
Effects of microtubule depolymerization brefeldin a induced golgi absorption into the er
Brefeldin A is a lactone antibiotic produced by fungal organisms such as Eupenicillium brefeldianum. Brefeldin A inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus indirectly by preventing association of coat COP-II protein to the golgi membrane. Brefeldin A was initially isolated as an anti-viral antibiotic but is now primarily used in biological research to study protein transport.
Contents
Physical data
Brefeldin A forms a clear colorless solution at 10 mg/ml in both dichloromethane and methanol.
Biological effects
In mammalian and yeast cells, the main target of brefeldin A appears to be a Guanine nucleotide exchange factor called GBF1. GBF1 mediates formation of transport vesicles by recruiting COPI coat proteins to cargo-bound receptor proteins found in the membrane of the Golgi. Inhibition of GBF1 activity induced the retrograde movement of secretory proteins from the golgi to the ER. The collapse of the Golgi into the ER triggers activation of unfolded protein response (UPR) (or ER stress) which can result in apoptosis.