Progress in K27 ubiquitin modification.

Author: Zhen SUN ¹ ; Hui LU ² ; Weidi XIAO ¹ ; Yanchang LI ¹ ; Ping XU ¹
Author Information

1. State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences (Beijing), Beijing Institute of Lifeomics, Beijing 102206, China.
2. Institute of Microbial Pharmaceuticals, College of Life and Health Sciences, Northeastern University, Shenyang 110819, Liaoning, China.
Publication Type:Journal Article
Keywords: DNA damage; K27 ubiquitin chain; immunity; ubiquitin
From: Chinese Journal of Biotechnology 2020;36(8):1484-1492
CountryChina
Language:Chinese
Abstract: Ubiquitination, one type of the most common post-translational modification, mediates the regulation of protein homeostasis in vivo. Since ubiquitin itself contains multiple lysine residues and one N-terminal free amino group, eight types of ubiquitin chains can be formed. The K27 ubiquitin chain is formed through the ubiquitination of the ubiquitin Lys27 (K27), which adopts a compact conformation. In recent years, biological function of the K27 ubiquitin chain in innate immunity, protein homeostasis and DNA damage has been discovered, but the molecular mechanisms of K27 ubiquitin chain assembly, recognition and hydrolysis are still poorly understood. Here we review the structural features and biological functions of K27 ubiquitin chain, to provide a reference for future studies.