Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization

Autor: Jorge Merlet, Lionel Pintard, José-Eduardo Gomes, Julien Burger
Přispěvatelé: Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), CNRS,JEG is funded by the Fundacao para a Ciencia a Tecnologia (ref:SFRH/BPD/21510/2005), Ministère de l'Education et de la Recherche, CNRS (ATIP program), FRM, ARC and the City of Paris
Rok vydání: 2009
Předmět:
Scaffold protein
Cell signaling
Saccharomyces cerevisiae Proteins
NEDD8 Protein
Protein subunit
macromolecular substances
COP9 Signalosome
Biology
NEDD8
Substrate Specificity
03 medical and health sciences
Cellular and Molecular Neuroscience
neddylation
0302 clinical medicine
Ubiquitin
Transcription (biology)
ubiquitin
dependent proteolysis
Animals
Drosophila Proteins
Phosphorylation
Molecular Biology
Ubiquitins
030304 developmental biology
Pharmacology
0303 health sciences
Arabidopsis Proteins
fungi
Ubiquitination
[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Molecular biology
Cell Biology
Cullin Proteins
Cell biology
Enzyme Activation
030220 oncology & carcinogenesis
biology.protein
Molecular Medicine
Neddylation
Protein Multimerization
deneddylation
Cullin
cullin-associated and neddylation-dissociated (CAND1)
Protein Binding
Zdroj: Cellular and Molecular Life Sciences
Cellular and Molecular Life Sciences, Springer Verlag, 2009, epub ahead of print. ⟨10.1007/s00018-009-8712-7⟩
ISSN: 1420-9071
1420-682X
DOI: 10.1007/s00018-009-8712-7⟩
Popis: International audience; Cullin-RING E3 ubiquitin-Ligases (CRLs) are the most prominent class of ubiquitin-ligases. By controlling the stability of a cohort of key regulators, CRLs impinge on many cellular and biological processes such as immunity, development, transcription, cell signalling and cell cycle progression. CRLs are multi-subunit complexes composed of a catalytic site and a substrate recognition module nucleated around a cullin scaffold protein. Most eukaryotic genomes encode at least five distinct cullins, and each of these cullins recruits a specific substrate-recognition module such that CRL complexes are modular. Despite their considerable diversity, CRLs are regulated by similar mechanisms. In particular, recent observations indicate that conformational variability induced by CRL dimerization and by conjugation of the ubiquitin-like protein NEDD8 on the cullin subunit stimulates substrate polyubiquitination. In this review, we discuss the composition of CRL complexes and the various molecular mechanisms controlling their activity.
Databáze: OpenAIRE
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