Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast
| Autor: | Kunio Nakatsukasa |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Saccharomyces cerevisiae Review macromolecular substances Endoplasmic-reticulum-associated protein degradation GPI-Linked Proteins Catalysis Inorganic Chemistry Ubc7 lcsh:Chemistry chemistry.chemical_compound Biosynthesis Ubc6 Physical and Theoretical Chemistry Ca2+/Mn2+ P-type ATPase Molecular Biology lcsh:QH301-705.5 Spectroscopy GPI-anchored protein biology Chemistry Endoplasmic reticulum Organic Chemistry Endoplasmic Reticulum-Associated Degradation General Medicine ERAD biology.organism_classification Doa10 Yeast Biosynthetic Pathways Computer Science Applications Cell biology Membrane protein lcsh:Biology (General) lcsh:QD1-999 Cytoplasm Hrd1 Protein Biosynthesis Protein folding |
| Zdroj: | International Journal of Molecular Sciences, Vol 22, Iss 1061, p 1061 (2021) International Journal of Molecular Sciences |
| ISSN: | 1661-6596 1422-0067 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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