Towards Understanding the Extensive Diversity of Protein N-glycan Structures in Eukaryotes

Overview

Journal Biol Rev Camb Philos Soc

Specialty Biology

Date 2021 Dec 7

PMID 34873817

Citations 12

Authors

Charlotte Toustou

Marie-Laure Walet-Balieu

Marie-Christine Kiefer-Meyer

Marine Houdou

Patrice Lerouge

Francois Foulquier

Muriel Bardor

Affiliations

Soon will be listed here.

Abstract

N-glycosylation is an important post-translational modification of proteins that has been highly conserved during evolution and is found in Eukaryota, Bacteria and Archaea. In eukaryotes, N-glycan processing is sequential, involving multiple specific steps within the secretory pathway as proteins travel through the endoplasmic reticulum and the Golgi apparatus. In this review, we first summarize the different steps of the N-glycan processing and further describe recent findings regarding the diversity of N-glycan structures in eukaryotic clades. This comparison allows us to explore the different regulation mechanisms of N-glycan processing among eukaryotic clades. Recent findings regarding the regulation of protein N-glycosylation are highlighted, especially the regulation of the biosynthesis of complex-type N-glycans through manganese and calcium homeostasis and the specific role of transmembrane protein 165 (TMEM165) for which homologous sequences have been identified in several eukaryotic clades. Further research will be required to characterize the function of TMEM165 homologous sequences in different eukaryotic clades.

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