Abstract
Ubiquitination, one of the most common posttranslational modifications of proteins, has a significant impact on its functions, such as stability, activity and cellular localization. Disorders in the processes of ubiquitination and deubiquitination are associated with various oncological and neurodegenerative diseases. The complexity of ubiquitin signaling – monoubiquitination and polyubiquitination with different lengths and types of interconnections between ubiquitins – determines their versatility and ability to regulate hundreds of different cellular processes. Advanced biochemical, mass spectrometric and computational methods are required for in-depth understanding of the mechanisms of assembly and disassembly, detection of ubiquitin chains and their signal transmission. Recent scientific achievements make it possible to identify the ubiquitination of proteins and the structure of ubiquitin chains, however, there are still a considerable number of unresolved issues in this area. Current review claims for a detailed analysis of the current understanding of the architectonics of the ubiquitin chains.
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