Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 290, Issue 35, Pages 21244-21251Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R115.675165
Keywords
E3 ubiquitin ligase; parkin; ubiquitin; ubiquitin ligase; ubiquitylation (ubiquitination); RING; cullin; ubiquitin regulation; HECT
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Funding
- National Institutes of Health through NIGMS [RO1 GM088055, R01 GM098503]
- National Institutes of Health through NCI [T32 CA080416]
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Since its discovery as a post-translational signal for protein degradation, our understanding of ubiquitin (Ub) has vastly evolved. Today, we recognize that the role of Ub signaling is expansive and encompasses diverse processes including cell division, the DNA damage response, cellular immune signaling, and even organismal development. With such a wide range of functions comes a wide range of regulatory mechanisms that control the activity of the ubiquitylation machinery. Ub attachment to substrates occurs through the sequential action of three classes of enzymes, E1s, E2s, and E3s. In humans, there are 2 E1s, approximate to 35 E2s, and hundreds of E3s that work to attach Ub to thousands of cellular substrates. Regulation of ubiquitylation can occur at each stage of the stepwise Ub transfer process, and substrates can also impact their own modification. Recent studies have revealed elegant mechanisms that have evolved to control the activity of the enzymes involved. In this minireview, we highlight recent discoveries that define some of the various mechanisms by which the activities of E3-Ub ligases are regulated.
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