Calnexin, More Than Just a Molecular Chaperone.

Autor: Paskevicius T; Department of Biochemistry, University of Alberta, Edmonton, AB T6G 2R3, Canada., Farraj RA; Department of Biochemistry, University of Alberta, Edmonton, AB T6G 2R3, Canada., Michalak M; Department of Biochemistry, University of Alberta, Edmonton, AB T6G 2R3, Canada., Agellon LB; School of Human Nutrition, McGill University, Sainte Anne de Bellevue, QC H9X 3V9, Canada.
Jazyk: angličtina
Zdroj: Cells [Cells] 2023 Jan 24; Vol. 12 (3). Date of Electronic Publication: 2023 Jan 24.
DOI: 10.3390/cells12030403
Abstrakt: 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.
Databáze: MEDLINE
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