Journal
JOURNAL OF BIOCHEMISTRY
Volume 161, Issue 2, Pages 125-133Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvw088
Keywords
acetylationmass spectrometry; post-translational modification; signal transduction; ubiquitin
Categories
Funding
- JSPS/MEXT KAKENHI Grant [JP24112004, JP16K14702, JP15H06882]
- Grants-in-Aid for Scientific Research [15H06882, 24112004] Funding Source: KAKEN
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Ubiquitylation is an essential post-translational modification (PTM) of proteins with diverse cellular functions. Polyubiquitin chains with different topologies have different cellular roles, and are referred to as a 'ubiquitin code'. Recent studies have begun to reveal that more complex ubiquitin architectures function as important signals in several biological pathways. These include PTMs of ubiquitin itself, such as acetylated ubiquitin and phospho-ubiquitin. Moreover, important roles for heterogeneous polyubiquitin chains, such as mixed or branched chains, have been reported, which significantly increase the diversity of the ubiquitin code. In this review, we describe mass spectrometry-based methods to characterize the ubiquitin signal. We also describe recent advances in our understanding of complex ubiquitin architectures, including our own findings concerning ubiquitin acetylation and branching within polyubiquitin chains.
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