Compartmentalization and Selective Tagging for Disposal of Misfolded Glycoproteins.

Autor: Shenkman M; School of Molecular Cell Biology and Biotechnology, George Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel., Lederkremer GZ; School of Molecular Cell Biology and Biotechnology, George Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel. Electronic address: gerardol@tauex.tau.ac.il.
Jazyk: angličtina
Zdroj: Trends in biochemical sciences [Trends Biochem Sci] 2019 Oct; Vol. 44 (10), pp. 827-836. Date of Electronic Publication: 2019 May 24.
DOI: 10.1016/j.tibs.2019.04.012
Abstrakt: The ability of mammalian cells to correctly identify and degrade misfolded secretory proteins, most of them bearing N-glycans, is crucial for their correct function and survival. An inefficient disposal mechanism results in the accumulation of misfolded proteins and consequent endoplasmic reticulum (ER) stress. N-glycan processing creates a code that reveals the folding status of each molecule, enabling continued folding attempts or targeting of the doomed glycoprotein for disposal. We review here the main steps involved in the accurate processing of unfolded glycoproteins. We highlight recent data suggesting that the processing is not stochastic, but that there is selective accelerated glycan trimming on misfolded glycoprotein molecules.
(Copyright © 2019 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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