2017年2月
The emerging complexity of ubiquitin architecture
JOURNAL OF BIOCHEMISTRY
- ,
- 巻
- 161
- 号
- 2
- 開始ページ
- 125
- 終了ページ
- 133
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1093/jb/mvw088
- 出版者・発行元
- OXFORD UNIV PRESS
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.
- リンク情報
- ID情報
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- DOI : 10.1093/jb/mvw088
- ISSN : 0021-924X
- eISSN : 1756-2651
- PubMed ID : 28011818
- Web of Science ID : WOS:000396969300002