Structural insights into N-linked glycan-mediated protein folding from chemical and biological perspectives

Taiki Kuribara; Kiichiro Totani

doi:10.1016/j.sbi.2020.11.004

Structural insights into N-linked glycan-mediated protein folding from chemical and biological perspectives

Curr Opin Struct Biol. 2021 Jun:68:41-47. doi: 10.1016/j.sbi.2020.11.004. Epub 2020 Dec 6.

Authors

Taiki Kuribara¹, Kiichiro Totani²

Affiliations

¹ Seikei University, 3-3-1 Kichijoji-kitamachi, Musashino-shi, Tokyo 180-8633, Japan.
² Seikei University, 3-3-1 Kichijoji-kitamachi, Musashino-shi, Tokyo 180-8633, Japan. Electronic address: ktotani@st.seikei.ac.jp.

PMID: 33296772
DOI: 10.1016/j.sbi.2020.11.004

Abstract

About half of all newly synthesized proteins have N-linked glycans. These glycans play pivotal roles in controlling the folding, sorting, and degradation of glycoproteins via several glycan-related proteins. The glycan-mediated protein quality control system is important for cellular homeostasis. In this review, we summarize recent advances in our understanding of the system and discuss structural insights from chemical and biological perspectives. In particular, we focus on the mechanisms by which these mediators respond to several folding states of glycoproteins.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Glycoproteins / metabolism
Polysaccharides*
Protein Folding*
Protein Transport

Substances

Glycoproteins
Polysaccharides