Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast

被引:9
作者
Nakatsukasa, Kunio [1 ]
机构
[1] Nagoya City Univ, Grad Sch Sci, Mizuho Ku, Yamanohata 1,Mizuho Cho, Nagoya, Aichi 4678501, Japan
关键词
ERAD; GPI-anchored protein; Hrd1; Doa10; Ubc6; Ubc7; Ca2+; Mn2+ P-type ATPase; Saccharomyces cerevisiae;
D O I
10.3390/ijms22031061
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
Misfolded and/or unassembled secretory and membrane proteins in the endoplasmic reticulum (ER) may be retro-translocated into the cytoplasm, where they undergo ER-associated degradation, or ERAD. The mechanisms by which misfolded proteins are recognized and degraded through this pathway have been studied extensively; however, our understanding of the physiological role of ERAD remains limited. This review describes the biosynthesis and quality control of glycosylphosphatidylinositol (GPI)-anchored proteins and briefly summarizes the relevance of ERAD to these processes. While recent studies suggest that ERAD functions as a fail-safe mechanism for the degradation of misfolded GPI-anchored proteins, several pieces of evidence suggest an intimate interaction between ERAD and the biosynthesis of GPI-anchored proteins.
引用
收藏
页码:1 / 14
页数:14
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