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- W4317933186 endingPage "403" @default.
- W4317933186 startingPage "403" @default.
- W4317933186 abstract "Calnexin is a type I integral endoplasmic reticulum (ER) membrane protein with an N-terminal domain that resides in the lumen of the ER and a C-terminal domain that extends into the cytosol. Calnexin is commonly referred to as a molecular chaperone involved in the folding and quality control of membrane-associated and secreted proteins, a function that is attributed to its ER- localized domain with a structure that bears a strong resemblance to another luminal ER chaperone and Ca2+-binding protein known as calreticulin. Studies have discovered that the cytosolic C-terminal domain of calnexin undergoes distinct post-translational modifications and interacts with a variety of proteins. Here, we discuss recent findings and hypothesize that the post-translational modifications of the calnexin C-terminal domain and its interaction with specific cytosolic proteins play a role in coordinating ER functions with events taking place in the cytosol and other cellular compartments." @default.
- W4317933186 created "2023-01-25" @default.
- W4317933186 creator A5014569062 @default.
- W4317933186 creator A5039383197 @default.
- W4317933186 creator A5039798650 @default.
- W4317933186 creator A5052943656 @default.
- W4317933186 date "2023-01-24" @default.
- W4317933186 modified "2023-10-14" @default.
- W4317933186 title "Calnexin, More Than Just a Molecular Chaperone" @default.
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