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Background
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Lactacystin is a specific inhibitor of the 26S proteasome, a high molecular weight, intracellular, multicatalytic, proteolytic complex that degrades ubiquitinated proteins, abnormal proteins and proteins in the endoplasmic reticulum. First isolated based upon its ability to induce differentiation in neuroblastoma cells, lactacystin is a cell-penetrating proteasome inhibitor that specifically inhibits the 26S proteasome by covalently binding to the active threonine residue in the amino-terminus of the catalytic beta subunit. Lactacystin has no effect on serine or cysteine proteases. Proteasome- mediated protein degradation is important in regulating a variety of cell processes, including the cell cycle, differentiation, apoptosis, cholesterol homeostasis and gene transcription.
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