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Calnexin, More Than Just a Molecular Chaperone.

Tautvydas PaskeviciusRabih Abou FarrajMarek MichalakLuis B Agellon
Published in: Cells (2023)
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 Ca 2+ -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.
Keyphrases
  • endoplasmic reticulum
  • binding protein
  • quality control
  • single molecule
  • estrogen receptor
  • breast cancer cells
  • oxidative stress
  • ultrasound guided
  • heat shock