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Free and N-Linked Oligomannosides as Markers of the Quality Control of Newly Synthesized Glycoproteins

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
258
Issue
1
Identifiers
DOI: 10.1006/bbrc.1999.0549
Keywords
  • N-Glycosylation
  • Endoplasmic Reticulum
  • Cytosol
  • Oligomannoside Trafficking
  • Quality Control
  • Protein Degradation
Disciplines
  • Biology

Abstract

Abstract It appears increasingly evident that the oligomannoside type N-glycans play important roles in the fate of newly synthesized glycoproteins in the rough endoplasmic reticulum. The variety of protein-bound oligomannoside isomers are involved in the quality control of glycoprotein, in their transport into the Golgi and probably as a degradation signal. A prerequisite of the degradation in the cytosol by the proteasome pathway is the release of the glycans as free oligomannosides. These oligomannosides are further processed in the cytosol into a peculiar isomer of Man 5GlcNAc 1which enters into the lysosome to be further degraded into monosaccharides. In this review, we will illustrate how the different species of N-linked and free oligomannosides either are involved or are markers of the quality control and fate of newly synthesized glycoproteins.

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