期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 44, 期 -, 页码 101-110出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2016.12.015
关键词
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资金
- Ciulli Laboratory at the University of Dundee
- European Research Council [ERC-2012-StG-311460]
- European Commission [H2020-MSCA-IF-2015-806323]
- Wellcome Trust [100476/Z/12/Z, 094090/Z/10/Z]
The ubiquitin-proteasome system is a master regulator of protein homeostasis, by which proteins are initially targeted for poly-ubiquitination by E3 ligases and then degraded into short peptides by the proteasome. Nature evolved diverse peptidic motifs, termed degrons, to signal substrates for degradation. We discuss degrons of the N-end rule pathway and also degrons characterized by post-translational modifications, including phosphorylation and hydroxylation. In each case we detail the structural basis of E3 ligase:degron recognition and small-molecule mimicry approaches that disrupt those protein protein interactions. We present as well genetic and chemical technologies that enable targeted degradation of proteins of interest, namely small-molecule dependent inducible degrons and chemical degraders, for example, proteolysis-targeting chimeras (PROTACs).
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