Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate
作者： E. D. Werner , J. L. Brodsky , A. A. McCracken
关键词: Proteasome 、 Cell biology 、 Endoplasmic-reticulum-associated protein degradation 、 Biochemistry 、 Microsome 、 Endoplasmic reticulum 、 Biology 、 Cytoplasm 、 Cytosol 、 Proteasome complex 、 Lactacystin
摘要: Until recently, the degradation of aberrant and unassembled proteins retained in endoplasmic reticulum (ER) was thought to involve unidentified ER-localized proteases. We now show that ER-associated (ERAD) two mutant accumulate ER lumen is inhibited a proteasome-defective yeast strain when cytosol from this used an vitro assay. In addition, ERAD limited presence proteasome inhibitors, 3,4-dichloroisocoumarin lactacystin. Furthermore, we find substrate exported ER-derived microsomes, accumulation 2-fold greater place wild-type cytosol. conclude lumenal substrates are cytoplasm for by complex.
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