Cargando…

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

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 st...

Descripción completa

Detalles Bibliográficos
Autor principal: Nakatsukasa, Kunio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7865462/
https://www.ncbi.nlm.nih.gov/pubmed/33494405
http://dx.doi.org/10.3390/ijms22031061
_version_ 1783647851741446144
author Nakatsukasa, Kunio
author_facet Nakatsukasa, Kunio
author_sort Nakatsukasa, Kunio
collection PubMed
description 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.
format Online
Article
Text
id pubmed-7865462
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-78654622021-02-07 Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast Nakatsukasa, Kunio Int J Mol Sci Review 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. MDPI 2021-01-21 /pmc/articles/PMC7865462/ /pubmed/33494405 http://dx.doi.org/10.3390/ijms22031061 Text en © 2021 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Nakatsukasa, Kunio
Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast
title Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast
title_full Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast
title_fullStr Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast
title_full_unstemmed Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast
title_short Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast
title_sort potential physiological relevance of erad to the biosynthesis of gpi-anchored proteins in yeast
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7865462/
https://www.ncbi.nlm.nih.gov/pubmed/33494405
http://dx.doi.org/10.3390/ijms22031061
work_keys_str_mv AT nakatsukasakunio potentialphysiologicalrelevanceoferadtothebiosynthesisofgpianchoredproteinsinyeast