Ubiquitin chain diversity at a glance

• Published in: Journal of cell science Vol. 129; no. 5; pp. 875 - 880
• Main Authors: Akutsu, Masato, Dikic, Ivan, Bremm, Anja
• Format: Journal Article
• Language: English
• Published: England 01.03.2016
• Subjects: Amino Acid Sequence; Animals; Humans; Immunity, Innate; Mitochondrial Degradation; Proteolysis; Signal Transduction; Ubiquitin - chemistry; Ubiquitin - physiology; Ubiquitination; Ubiquitin; Ubiquitin chains; Phospho-ubiquitin; Atypical ubiquitin linkages
• ISSN: 0021-9533; 1477-9137
• DOI: 10.1242/jcs.183954

Ubiquitin plays an essential role in modulating protein functions, and deregulation of the ubiquitin system leads to the development of multiple human diseases. Owing to its molecular features, ubiquitin can form various homo- and heterotypic polymers on substrate proteins, thereby provoking distinct cellular responses. The concept of multifaceted ubiquitin chains encoding different functions has been substantiated in recent years. It has been established that all possible ubiquitin linkage types are utilized for chain assembly and propagation of specific signals in vivo. In addition, branched ubiquitin chains and phosphorylated ubiquitin molecules have been put under the spotlight recently. The development of novel technologies has provided detailed insights into the structure and function of previously poorly understood ubiquitin signals. In this Cell Science at a Glance article and accompanying poster, we provide an update on the complexity of ubiquitin chains and their physiological relevance.