Electrostatic and steric effects underlie acetylation-induced changes in ubiquitin structure and function.

ABSTRACT: Covalent attachment of ubiquitin (Ub) to proteins is a highly versatile posttranslational modification. Moreover, Ub is not only a modifier but itself is modified by phosphorylation and lysine acetylation. However, the functional consequences of Ub acetylation are poorly understood. By generation and comprehensive characterization of all seven possible mono-acetylated Ub variants, we show that each acetylation site has a particular impact on Ub structure. This is reflected in selective usage of the acetylated variants by different E3 ligases and overlapping but distinct interactomes, linking different acetylated variants to different cellular pathways. Notably, not only electrostatic but also steric effects contribute to acetylation-induced changes in Ub structure and, thus, function. Fina

SUBMITTER: Kienle SM 

PROVIDER: S-EPMC9481602 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature