| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8304507 | Biochimie | 2016 | 9 Pages |
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
deubiquitylating enzymeSpsbSkp2DUBCSNS-phase kinase-associated protein 2β-TrCPFbw7MRE11DDB1NEDD8CAND1HECTSkp1TNF-R2ELOLatency-associated nuclear antigenCullin RING ligaseRBxE2 ubiquitin-conjugating enzymemeiotic recombination 11S-PHASE KINASE-ASSOCIATED PROTEIN 1Kaposi's sarcoma-associated herpes virusRING box proteinBTBROCMALFAKVIFNAEWSBIRSJAK2VHLSOCSMLLJanus Kinase 2LANAKSHVCRLE3 ubiquitin ligasevon Hippel-Lindauinsulin receptor substrateTherapeutic targetsRingsuppressors of cytokine signalingUbiquitin-proteasome systemviral infectivity factorASBMixed lineage leukemiaHIV-1human immunodeficiency virus-1really interesting new genefocal adhesion kinasetumor necrosis factor receptor 2
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Authors
Isabelle Lamsoul, Sandrine Uttenweiler-Joseph, Christel Moog-Lutz, Pierre G. Lutz,