Endoplasmic reticulum stress differentially inhibits endoplasmic reticulum and inner nuclear membrane protein quality control degradation pathways
نویسندگان
چکیده
منابع مشابه
Glycoprotein Quality Control and Endoplasmic Reticulum Stress.
The endoplasmic reticulum (ER) supports many cellular processes and performs diverse functions, including protein synthesis, translocation across the membrane, integration into the membrane, folding, and posttranslational modifications including N-linked glycosylation; and regulation of Ca2+ homeostasis. In mammalian systems, the majority of proteins synthesized by the rough ER have N-linked gl...
متن کاملProtein quality control in the endoplasmic reticulum
THE TOPOLOGICAL BARRIERS DEFINED BY BIOLOGICAL MEMBRANES ARE NOT IMPERMEABLE: from small solutes to intact proteins, specialized transport and translocation mechanisms adjust to the cell's needs. Here, we review the removal of unwanted proteins from the endoplasmic reticulum (ER) and emphasize the need to extend observations from tissue culture models and simple eukaryotes to studies in whole a...
متن کاملTargeting pathways to the endoplasmic reticulum membrane.
The targeting of proteins to the endoplasmic reticulum (ER) membrane is the first step in the secretory pathway through which proteins are transported to the outside of the cell, the plasma membrane, and the luminal spaces and membranes of the endomembrane system. Proteins that undergo this targeting event carry a stretch of hydrophobic amino acids, usually at the amino terminus, that constitut...
متن کاملThe unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane.
The endoplasmic reticulum (ER) is a multifunctional organelle responsible for production of both lumenal and membrane components of secretory pathway compartments. Secretory proteins are folded, processed, and sorted in the ER lumen and lipid synthesis occurs on the ER membrane itself. In the yeast Saccharomyces cerevisiae, synthesis of ER components is highly regulated: the ER-resident protein...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2019
ISSN: 0021-9258
DOI: 10.1074/jbc.ra119.010295