Cullin 5-RING E3 ubiquitin ligases, new therapeutic targets?

Isabelle Lamsoul; Sandrine Uttenweiler-Joseph; Christel Moog-Lutz; Pierre G Lutz

doi:10.1016/j.biochi.2015.08.003

Cullin 5-RING E3 ubiquitin ligases, new therapeutic targets?

Biochimie. 2016 Mar:122:339-47. doi: 10.1016/j.biochi.2015.08.003. Epub 2015 Aug 4.

Authors

Isabelle Lamsoul¹, Sandrine Uttenweiler-Joseph¹, Christel Moog-Lutz¹, Pierre G Lutz²

Affiliations

¹ CNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), 205 route de Narbonne, BP 64182, F-31077 Toulouse, France; Université de Toulouse, UPS, IPBS, F-31077 Toulouse, France.
² CNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), 205 route de Narbonne, BP 64182, F-31077 Toulouse, France; Université de Toulouse, UPS, IPBS, F-31077 Toulouse, France. Electronic address: Pierre.Lutz@ipbs.fr.

PMID: 26253693
DOI: 10.1016/j.biochi.2015.08.003

Abstract

Ubiquitylation is a reversible post-translational modification of proteins that controls a myriad of functions and cellular processes. It occurs through the sequential action of three distinct enzymes. E3 ubiquitin ligases (E3s) play the role of conductors of the ubiquitylation pathway making them attractive therapeutic targets. This review is dedicated to the largest family of multimeric E3s, the Cullin-RING E3 (CRL) family and more specifically to cullin 5 based CRLs that remains poorly characterized.

Keywords: Cullin RING ligase; E3 ubiquitin ligase; Therapeutic targets; Ubiquitin-proteasome system.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Antineoplastic Agents / therapeutic use
Cullin Proteins / metabolism*
Humans
Models, Biological
Neoplasms / drug therapy
Neoplasms / metabolism
Proteasome Endopeptidase Complex / metabolism*
Signal Transduction / drug effects
Ubiquitin / metabolism
Ubiquitin-Protein Ligases / metabolism*
Ubiquitination*

Substances

Antineoplastic Agents
CUL5 protein, human
Cullin Proteins
Ubiquitin
Ubiquitin-Protein Ligases
Proteasome Endopeptidase Complex