Related Experiment Video
Updated: Jul 4, 2026
06:55
Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
Published on: June 7, 2020
The interaction network of the chaperonin CCT
Carien Dekker1, Peter C Stirling, Elizabeth A McCormack
1Cancer Research UK Centre for Cell and Molecular Biology, Chester Beatty Laboratories, Institute of Cancer Research, London, UK.
The EMBO Journal
|May 31, 2008
Summary
The eukaryotic chaperonin containing TCP-1 (CCT) aids protein folding, maintaining cell stability. This study reveals CCT
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The eukaryotic cytosolic chaperonin containing TCP-1 (CCT) is crucial for cellular homeostasis.
- CCT assists in folding essential proteins like actin and tubulin, but its full network of interactions and dependent pathways remain largely undefined.
- Understanding CCT's global function is vital for comprehending fundamental cellular processes.
Purpose of the Study:
- To globally define the protein and genetic interaction networks of CCT.
- To identify novel cellular pathways and systems regulated by CCT.
- To elucidate the role of CCT in cytoskeletal organization and cell division.
Main Methods:
- Proteomic analysis to identify CCT-interacting proteins.
- Genomic approaches to map CCT-dependent genes.
- Functional assays in yeast to study CCT-septin interactions and septin ring assembly.
Main Results:
- Identified interaction networks involving 136 proteins/genes linked to CCT.
- Established connections between CCT and the nuclear pore complex, chromatin remodeling, and protein degradation pathways.
- Discovered a novel CCT-dependent eukaryotic cytoskeletal system: the septin ring complex, essential for cytokinesis.
- Demonstrated that CCT-septin interactions are ATP-dependent and crucial for proper septin ring assembly in yeast.
Conclusions:
- CCT plays a broader role in cellular organization than previously known, extending to epigenetics and cell division.
- The study provides a comprehensive framework for understanding CCT's multifaceted functions in essential cellular processes.
- Disruption of CCT function leads to defects in septin ring assembly, highlighting its importance in cytokinesis.
Related Concept Videos
03:00Molecular Chaperones and Protein Folding
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
03:00Molecular Chaperones and Protein Folding
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
02:26Protein Networks
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
02:26Protein Networks
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
01:43Electron Transport Chain: Complex III and IV
During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
02:41Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...