ArticleMolecular biology of the cell2002
Organizational diversity among distinct glycoprotein endoplasmic reticulum-associated degradation programs.
Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 109 citations in OpenAlex.
- Manipulation of Proteostasis Networks in Transgenic ZAAT Zebrafish via CRISPR-Cas9 Gene Editing.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Expression of the Z Variant of α1-Antitrypsin Suppresses Hepatic Cholesterol Biosynthesis in Transgenic Zebrafish.International journal of molecular sciences · 2023Article
- Z-αScience advances · 2022Article
- ILDR2 stabilization is regulated by its interaction with GRP78.Scientific reports · 2021Article
- Calreticulin enhances the secretory trafficking of a misfolded α-1-antitrypsin.The Journal of biological chemistry · 2020Article
- Modulation of calreticulin expression reveals a novel exosome-mediated mechanism of Z variant αThe Journal of biological chemistry · 2019Article
- Erdj3 Has an Essential Role for Z Variant Alpha-1-Antitrypsin Degradation.Journal of cellular biochemistry · 2017Article
- OS-9 facilitates turnover of nonnative GRP94 marked by hyperglycosylation.Molecular biology of the cell · 2014Article
- Glycoprotein folding and quality-control mechanisms in protein-folding diseases.Disease models & mechanisms · 2014Review
- Advances in alpha-1-antitrypsin deficiency liver disease.Current gastroenterology reports · 2014Review
- Golgi-situated endoplasmic reticulum α-1, 2-mannosidase contributes to the retrieval of ERAD substrates through a direct interaction with γ-COP.Molecular biology of the cell · 2013Article
- Article
- Histone deacetylase inhibitor (HDACi) suberoylanilide hydroxamic acid (SAHA)-mediated correction of α1-antitrypsin deficiency.The Journal of biological chemistry · 2012Article
- The endosomal protein-sorting receptor sortilin has a role in trafficking α-1 antitrypsin.Genetics · 2012Article
- The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology.Physiological reviews · 2012Review
- Golgi localization of ERManI defines spatial separation of the mammalian glycoprotein quality control system.Molecular biology of the cell · 2011Article
- Proteostasis: a new therapeutic paradigm for pulmonary disease.Proceedings of the American Thoracic Society · 2011Article
- Hepatic fibrosis and carcinogenesis in α1-antitrypsin deficiency: a prototype for chronic tissue damage in gain-of-function disorders.Cold Spring Harbor perspectives in biology · 2011Review
- Mechanisms underlying the cellular clearance of antitrypsin Z: lessons from yeast expression systems.Proceedings of the American Thoracic Society · 2010Article
- Intracellular processing of alpha1-antitrypsin.Proceedings of the American Thoracic Society · 2010Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Protein folding and quality control in the early secretory pathway function as posttranslational checkpoints in eukaryote gene expression. Herein, an aberrant form of the hepatic secretory protein alpha1-antitrypsin was stably expressed in a human embryonic kidney cell line to elucidate the mechanisms by which glycoprotein endoplasmic reticulum-associated degradation (GERAD) is administered in cells from higher eukaryotes. After biosynthesis, genetic variant PI Z underwent alternative phases of secretion and degradation, the latter of which was mediated by the proteasome. Degradation required release from calnexin- and asparagine-linked oligosaccharide modification by endoplasmic reticulum mannosidase I, the latter of which occurred as PI Z was bound to the molecular chaperone grp78/BiP. That a distinct GERAD program operates in human embryonic kidney cells was supported by the extent of PI Z secretion, apparent lack of polymerization, inability of calnexin to participate in the degradation process, and sequestration of the glycoprotein folding sensor UDP-glucose:glycoprotein glucosyltransferase in the Golgi complex. Because UDP-glucose:glycoprotein glucosyltransferase sustains calnexin binding, its altered distribution is consistent with a GERAD program that hinders the reentry of substrates into the calnexin cycle, allowing grp78/BiP to partner with a lectin, other than calnexin, in the recognition of a two-component GERAD signal to facilitate substrate recruitment. How the processing of a mutant protein, rather than the mutation itself, can contribute to disease pathogenesis, is discussed.
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