Please use this identifier to cite or link to this item:
Title: Regulation of Cullin E3 Ubiquitin Ligases By the Ubiquitin Like Protein Nedd8 and Cullin-Interacting Proteins
Keywords: Cullin RING ligase, Nedd8, CAND1, CSN, Cycle Inhibiting Factor, Rbx1
Issue Date: 13-Jan-2012
Citation: BOH BOON KIM (2012-01-13). Regulation of Cullin E3 Ubiquitin Ligases By the Ubiquitin Like Protein Nedd8 and Cullin-Interacting Proteins. ScholarBank@NUS Repository.
Abstract: Cullin RING ubiquitin ligases (CRLs) constitute the largest family of cellular ubiquitin ligases that mediate polyubiquitination of numerous cellular substrates. In this study, I characterized the mechanistic regulation of CRLs. My findings support the hypothesis that CAND1 does not function by sequestering cullins in vivo to prevent substrate receptor autoubiquitination and is likely to regulate CRLs activity via alternative mechanisms. Substantially, I studied the mechanism of Nedd8-induced CRL activation in vivo by demonstrating that in vivo neddylation functions by inducing conformational changes in the C-terminal domain of cullins that free the RING domain of Rbx1 and bridge the gap for ubiquitin transfer onto the substrate. I provided evidence as well on a bacteria effector protein, known as Cycle Inhibitng Factor (Cif), in inhibiting CRLs by interfering with Nedd8-induced conformational control, which is dependent on the interaction between the Nedd8 hydrophobic patch and the cullin winged-helix B subdomain.
Appears in Collections:Ph.D Theses (Open)

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
BohBK THESIS NUS 2012.pdf6.88 MBAdobe PDF



Google ScholarTM


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.