Compartmentalization and Selective Tagging for Disposal of Misfolded Glycoproteins

Marina Shenkman, Gerardo Z. Lederkremer*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review


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.

Original languageEnglish
Pages (from-to)827-836
Number of pages10
JournalTrends in Biochemical Sciences
Issue number10
StatePublished - Oct 2019


  • EDEM
  • ER quality control
  • ERAD
  • OS-9
  • calnexin
  • mannosidase


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