Glycoprotein Quality Control and Endoplasmic Reticulum Stress
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...
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The ER is one of the most important folding compartments within the cell, as well as an intracellular Ca(2+) storage organelle and it contains a number of Ca(2+) regulated molecular chaperones responsible for the proper folding of glycosylated as well as non-glycosylated proteins. The luminal environment of the ER contains Ca(2+) which is involved in regulating chaperones such as calnexin and c...
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In cells, the quality of newly synthesized proteins is monitored with endoplasmic reticulum quality control (ERQC) in regard to proper folding and correct assembly in the early secretory pathway. Sequential checkpoints are distributed along the early secretory pathway, allowing efficiency and fidelity in protein secretion. Recently, ERQC has been mathematically modeled by breaking it into three...
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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 کاملThe evolution of N-glycan-dependent endoplasmic reticulum quality control factors for glycoprotein folding and degradation.
Asn-linked glycans (N-glycans) play important roles in the quality control (QC) of glycoprotein folding in the endoplasmic reticulum (ER) lumen and in ER-associated degradation (ERAD) of proteins by cytosolic proteasomes. A UDP-Glc:glycoprotein glucosyltransferase glucosylates N-glycans of misfolded proteins, which are then bound and refolded by calreticulin and/or calnexin in association with ...
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ژورنال
عنوان ژورنال: Molecules
سال: 2015
ISSN: 1420-3049
DOI: 10.3390/molecules200813689