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Emerging Roles and Research Tools of Atypical Ubiquitination
Author(s) -
Huang Qiuling,
Zhang Xiaofei
Publication year - 2020
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201900100
Subject(s) - ubiquitin , autophagy , microbiology and biotechnology , deubiquitinating enzyme , ubiquitin ligase , ubiquitin conjugating enzyme , biology , signal transduction , ubiquitin protein ligases , computational biology , posttranslational modification , chemistry , biochemistry , enzyme , gene , apoptosis
Ubiquitination is a posttranslational modification characterized by the covalent attachment of ubiquitin molecules to protein substrates. The ubiquitination modification process is reversible, dynamic, and involved in the regulation of various biological processes, such as autophagy, inflammatory responses, and DNA damage responses. The forms of ubiquitin modification are very diverse, incorporating either a single ubiquitin molecule or a complicated ubiquitin polymer, and different types of ubiquitination usually elicit corresponding cellular responses. The development of research tools and strategies has afforded more detailed insight into atypical ubiquitin signaling pathways that were previously poorly understood. Here, an update on the understanding of atypical ubiquitin chain signaling pathways is provided and the recent development of representative research tools for ubiquitin systems is discussed. In addition, the future challenges in ubiquitin research are reflected on and summarized.