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Multiple quality control mechanisms monitor yeast chitin synthase folding in the endoplasmic reticulum.
Mol Biol Cell
December 2023
Instituto de Biología Funcional y Genómica (IBFG) and Departamento de Microbiología y Genética, CSIC-Universidad de Salamanca, 37007 Salamanca, Spain.
Article Synopsis
- Chitin synthase Chs3 is a complex protein that must be properly folded to exit the endoplasmic reticulum (ER), with its stability in the ER suggesting limited recognition by quality control systems.
- Proper N-glycosylation of Chs3's luminal domain prevents protein aggregation and protects it from degradation by the Hrd1-dependent ERAD-L pathway.
- Additionally, Chs3 interacts with its chaperone Chs7 to hide degradation signals, allowing misfolded proteins to be sorted to the inner nuclear membrane for degradation by the INMAD system, making Chs3 a key model for studying cellular quality control processes.
Degradation of integral membrane proteins modified with the photosensitive degron module requires the cytosolic endoplasmic reticulum-associated degradation pathway.
Mol Biol Cell
September 2019
Department of Biology/Genetics, Philipps-University Marburg, 35043 Marburg, Germany.
Protein quality mechanisms are fundamental for proteostasis of eukaryotic cells. Endoplasmic reticulum-associated degradation (ERAD) is a well-studied pathway that ensures quality control of secretory and endoplasmic reticulum (ER)-resident proteins. Different branches of ERAD are involved in degradation of malfolded secretory proteins, depending on the localization of the misfolded part, the ER lumen (ERAD-L), the ER membrane (ERAD-M), and the cytosol (ERAD-C).
View Article and Find Full Text PDFThe yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron.
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April 2015
Department of Biology, University of Konstanz, 78457 Konstanz, Germany
Aberrant endoplasmic reticulum (ER) proteins are eliminated by ER-associated degradation (ERAD). This process involves protein retrotranslocation into the cytosol, ubiquitylation, and proteasomal degradation. ERAD substrates are classified into three categories based on the location of their degradation signal/degron: ERAD-L (lumen), ERAD-M (membrane), and ERAD-C (cytosol) substrates.
View Article and Find Full Text PDFThe SUD1 gene encodes a putative E3 ubiquitin ligase and is a positive regulator of 3-hydroxy-3-methylglutaryl coenzyme a reductase activity in Arabidopsis.
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Instituto de Hortofruticultura Subtropical y Mediterránea, Universidad de Málaga-Consejo Superior de Investigaciones Científicas, Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Universidad de Málaga, 29071 Malaga, Spain.
The 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) enzyme catalyzes the major rate-limiting step of the mevalonic acid (MVA) pathway from which sterols and other isoprenoids are synthesized. In contrast with our extensive knowledge of the regulation of HMGR in yeast and animals, little is known about this process in plants. To identify regulatory components of the MVA pathway in plants, we performed a genetic screen for second-site suppressor mutations of the Arabidopsis thaliana highly drought-sensitive drought hypersensitive2 (dry2) mutant that shows decreased squalene epoxidase activity.
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