Tyrosinase degradation via two pathways during reverse translocation to the cytosol

被引:20
作者
Mosse, CA
Hsu, W
Engelhard, VH
机构
[1] Univ Virginia, Carter Immunol Ctr, Charlottesville, VA 22908 USA
[2] Univ Virginia, Dept Microbiol, Charlottesville, VA 22908 USA
关键词
protein degradation; tyrosinase; endoplasmic reticulum; antigen processing; deglycosylation;
D O I
10.1006/bbrc.2001.5153
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Previous studies established that after inhibition of proteasome activity, tyrosinase could be detected in the cytosol after initial translation in the endoplasmic reticulum (ER), with a molecular weight consistent with that of a full-length, deglycosylated polypeptide. Here we show that most of these molecules are glycosylated, but have been proteolyzed at the carboxyl terminus by a protease that is insensitive to proteasome inhibitors. We also demonstrate the inhibitor-dependent accumulation of a membrane species that appears structurally homologous to the glycosylated and partially proteolyzed cytosolic form. Under some circumstances, cytosolic tyrosinase that had been deglycosylated and not proteolyzed prior to proteasomal degradation could also be detected. The presence of cytosolic tyrosinase was dependent upon Glycosylation of the molecule during synthesis in the ER. These results suggest the existence of at least two alternative pathways for degradation of tyrosinase in the cytosol. (C) 2001 Academic Press.
引用
收藏
页码:313 / 319
页数:7
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