Aufklärung der Strukturen und Mechanismen von großen nicht-kanonischen Cullin-RING-Ligasen
Year: 2024
Type: dissertation
Abstract: This study elucidates structures and mechanisms of complexes formed by the two non-canonical cullin-RING ubiquitin E3 ligases (CRLs), CUL7 and CUL9. CUL7 forms a unique CRL E3-E3 assembly that inverts classic roles, with CUL7 acting as substrate receptor and the F-box protein as adaptor, linking to the catalytical CUL1-RBX1 complex, mediating TP53 ubiquitylation. CUL9 forms a 1.8 MDa hexameric assembly that unifies two E3 ligase classes (cullin-RING and RBR) in one complex. Our studies opened a new chapter on how CRLs use E3-E3 super-assemblies for substrate ubiquitylation.
Authors: Hopf, Linus Valentin Moritz, Schulman, Brenda A. 1967-, Technische Universität München
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W6989388483