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Subcell Biochem. 2017;83:323-347. doi: 10.1007/978-3-319-46503-6_12.

Cullin-RING E3 Ubiquitin Ligases: Bridges to Destruction.

Author information

1
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06511, USA.
2
Department of Biochemistry and Biophysics, University of California, San Francisco, CA, 94158, USA.
3
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06511, USA. yong.xiong@yale.edu.

Abstract

Ubiquitination is a highly conserved post-translational modification in eukaryotes, well known for targeting proteins for degradation by the 26S proteasome. Proteins destined for proteasomal degradation are selected by E3 ubiquitin ligases. Cullin-RING E3 ubiquitin ligases (CRLs) are the largest superfamily of E3 ubiquitin ligases, with over 400 members known in mammals. These modular complexes are tightly regulated in the cell. In this chapter, we highlight recent structural and biochemical advances shedding light on the assembly and architecture of cullin-RING ligases, their dynamic regulation by a variety of host factors, and their manipulation by viral pathogens and small molecules.

KEYWORDS:

Cullin; Cullin-RING ligase; E3 ligase; NEDD8; Neddylation; Protein-protein interaction; Ubiquitin; Ubiquitination; Ubiquitylation; Viral hijacking

PMID:
28271482
DOI:
10.1007/978-3-319-46503-6_12
[Indexed for MEDLINE]

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