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Exiting the endoplasmic reticulum
Molecular and Cellular Endocrinology, 2001The movement of nascent proteins from sites of synthesis to final cellular or extracellular destinations involves their transport through a distinct series of vesicular compartments. Vesicle biogenesis is regulated by specific proteins and co-factors that control distinct steps including budding, transport, docking, and fusion with target membranes ...
F S, Gorelick, C, Shugrue
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Exiting the Endoplasmic Reticulum
Traffic, 2005Vesicular transport from the endoplasmic reticulum (ER) to the Golgi complex constitutes the initial step in protein secretion. COPII‐coated vesicles mediate the export of newly synthesized proteins from the ER, and this transport step is coupled with COPI‐mediated retrograde traffic to form a transport circuit that supports the compositional asymmetry
Joseph D, Mancias, Jonathan, Goldberg
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ENDOPLASMIC RETICULUM–ASSOCIATED DEGRADATION
Annual Review of Cell and Developmental Biology, 2005Secretory and transmembrane proteins enter the secretory pathway through the protein-conducting Sec61 channel in the membrane of the endoplasmic reticulum. In the endoplasmic reticulum, proteins fold, are frequently covalently modified, and oligomerize before they are packaged into transport vesicles that shuttle them to the Golgi complex.
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Sensing Endoplasmic Reticulum Stress
2012This chapter provides an overview of our present understanding of mechanisms of sensing protein folding status and endoplasmic reticulum (ER) stress in eukaryotic cells. The ER folds and matures most secretory and transmembrane proteins. Mis- or unfolded proteins are sensed by specialized ER stress sensors, such as IRE1, PERK and ATF6, which initiate ...
Vipul M, Parmar, Martin, Schröder
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Endoplasmic reticulum stress and unfolded protein response in cardiovascular diseases
Nature Reviews Cardiology, 2021Jun Ren +4 more
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Endoplasmic reticulum stress responses
Cellular and Molecular Life Sciences, 2007In homeostasis, cellular processes are in a dynamic equilibrium. Perturbation of homeostasis causes stress. In this review I summarize how perturbation of three major functions of the endoplasmic reticulum (ER) in eukaryotic cells -- protein folding, lipid and sterol biosynthesis, and storing intracellular Ca(2+) -- causes ER stress and activates ...
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Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes
Science, 2004Umut Özcan +9 more
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Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
Nature, 1999H. Harding, Yuhong Zhang, D. Ron
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