Related Experiment Video
Updated: Jan 14, 2026

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
Published on: March 14, 2019
The many faces of the GID/CTLH E3 ligase complex
Arno F Alpi1,2, Jakub Chrustowicz1, Dawafuti Sherpa1
1Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, 82152, Germany.
The GID/C-terminal to LisH (CTLH) E3 ligase complex is a versatile regulator of cellular processes. Its adaptable structure and regulatory mechanisms offer potential for targeted protein degradation therapies.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- The GID/C-terminal to LisH (CTLH) E3 ligase complex is an evolutionarily conserved multiprotein complex.
- It plays crucial roles in metabolic rewiring, stress response, differentiation, and immunity.
Purpose of the Study:
- To review the distinct features of GID/CTLH E3 ubiquitin ligases.
- To examine the mechanistic implications of their regulation and substrate targeting.
- To discuss their therapeutic potential in targeted protein degradation.
Main Methods:
- Biochemical reconstitution
- Cryo-electron microscopy (cryo-EM)
- Cell-based studies
Main Results:
- GID/CTLH E3 complexes exhibit dynamic composition and structure.
- Regulation occurs via interchangeable substrate receptors and supramolecular assembly factors.
- Paralogous subunits and regulatory factors fine-tune substrate selection and function.
Conclusions:
- The GID/CTLH E3 system demonstrates remarkable adaptability and sophisticated regulation.
- Its ability to target oligomeric substrates is mechanistically significant.
- It holds promise for therapeutic applications in targeted protein degradation.
More Related Videos
10:11Author Spotlight: Investigating the Motion Dynamics of the Eukaryotic Replisome Components at the Single-Molecule Level
Published on: July 26, 2024
05:28Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay
Published on: September 10, 2020
Related Concept Videos
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
Coat Assembly and GTPases
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Activation and Inactivation of G Proteins
GTPases and their Regulation
GTPases and their Regulation
Large G-proteins,...