Building and remodelling Cullin-RING E3 ubiquitin ligases.
Cullin-RING E3 ubiquitin ligases (CRLs) control a plethora of biological pathways through targeted ubiquitylation of signalling proteins. These modular assemblies use substrate receptor modules to recruit specific targets. Recent efforts have focused on understanding the mechanisms that control the activity state of CRLs through dynamic alterations in CRL architecture. Central to these processes are cycles of cullin neddylation and deneddylation, as well as exchange of substrate receptor modules to re-sculpt the CRL landscape, thereby responding to the cellular requirements to turn over distinct proteins in different contexts. This review is focused on how CRLs are dynamically controlled with an emphasis on how cullin neddylation cycles are integrated with receptor exchange.
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
John R
JR
Lydeard
Brenda A
BA
Schulman
J Wade
JW
Harper
D000595:Amino Acid Sequence; D000818:Animals; D000075686:COP9 Signalosome Complex; D044842:Cullin Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry / Q000378:metabolism; D010447:Peptide Hydrolases / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D014157:Transcription Factors / Q000378:metabolism; D014452:Ubiquitins / Q000737:chemistry / Q000378:metabolism*
D044842:Cullin Proteins; D046912:Multiprotein Complexes; D014157:Transcription Factors; D014452:Ubiquitins; D010447:Peptide Hydrolases; D000075686:COP9 Signalosome Complex