RRC ID 74187
Author Nakatsukasa K.
Title Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast.
Journal Int J Mol Sci
Abstract 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.
Volume 22(3)
Published 2021-1-21
DOI 10.3390/ijms22031061
PII ijms22031061
PMID 33494405
PMC PMC7865462
MeSH Biosynthetic Pathways Endoplasmic Reticulum-Associated Degradation* GPI-Linked Proteins / biosynthesis* Protein Biosynthesis* Saccharomyces cerevisiae / physiology* Saccharomyces cerevisiae Proteins / genetics Saccharomyces cerevisiae Proteins / metabolism
IF 4.556
Yeast BY23849