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Original title:
Mechanistic studies of GID/CTLH E3 ubiquitin ligases
Translated title:
Mechanistische Untersuchungen der GID/CTLH E3 Ubiquitinligasen
Author:
Chrustowicz, Jakub
Year:
2022
Document type:
Dissertation
Faculty/School:
Fakultät für Chemie
Advisor:
Schulman, Brenda (Prof., Ph.D.)
Referee:
Schulman, Brenda (Prof., Ph.D.); Sattler, Michael (Prof. Dr.); Dikic, Ivan (Prof., Ph.D.)
Language:
en
Subject group:
CHE Chemie
Keywords:
ubiquitin, E3 ligase, N-degron, GID, CTLH
TUM classification:
CHE 800
Abstract:
The integrative structural, biochemical, and cell biology data revealed mechanistic principles of substrate targeting by evolutionarily conserved GID/CTLH E3 ubiquitin ligases. The pliable substrate receptors adapt their conformations to recognize various N-terminal peptide/degron sequences, whereas the chelator-like supramolecular assembly of a catalytically active E3 ligase core configures multi-pronged targeting of oligomeric substrates. The revealed principles provide a conceptual framework...     »
Translated abstract:
Die integrativen, strukturellen, biochemischen und zellbiologischen Experimente gaben Aufschluss über mechanistische Prinzipien der Substratausrichtung von evolutionär konservierten GID/CTLH E3 Ubiquitinligasen. Die flexiblen Substratrezeptoren passen ihre Konformationen an um verschiedene N-terminale Peptide bzw. Degrons zu erkennen, während der Chelator-ähnliche supermolekulare Komplex eines aktiven E3 Ligase Kerns für die mehrgleisige Ubiquitinierung von oligomeren Substraten sorgt. Die darge...     »
WWW:
https://mediatum.ub.tum.de/?id=1633713
Date of submission:
23.11.2021
Oral examination:
11.02.2022
File size:
11744848 bytes
Pages:
81
Urn (citeable URL):
https://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:91-diss-20220211-1633713-1-4
Last change:
21.03.2022
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