Abstract
Protein ubiquitylation is an essential post-translational modification that regulates various cellular functions such as protein degradation, signal transduction, DNA repair, and protein sorting. Behind this versatile function of ubiquitylation lies the myriad structural diversity formed by a combination of 8 ubiquitin-ubiquitin linkages, chain lengths, and post-translational modifications, and functional information embedded in different ubiquitin architecture is referred to as the ubiquitin code. Elucidation of the ubiquitin code is important for understanding the pathogenic mechanism of numerous ubiquitin-related diseases and for developing chemical protein degraders such as PROTAC. Here, We review recent advances in analyzing methods of the ubiquitin chain architecture and its application for chemical degraders.
