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Related Concept Videos

Protein Networks02:26

Protein Networks

4.6K
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,...
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Protein Networks02:26

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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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Molecular Chaperones and Protein Folding03:00

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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...
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Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Updated: Feb 23, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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Features of the Chaperone Cellular Network Revealed through Systematic Interaction Mapping.

Kamran Rizzolo1, Jennifer Huen1, Ashwani Kumar2

  • 1Department of Biochemistry, University of Toronto, Toronto, ON M5G 1M1, Canada.

Cell Reports
|September 14, 2017
PubMed
Summary

Researchers mapped the molecular chaperone network in yeast, discovering a large supercomplex named the naturally joined (NAJ) chaperone complex. This reveals distinct chaperone roles in maintaining protein homeostasis.

Keywords:
Hsp90NAJ chaperone complexR2TPRvb1Rvb2chaperone networkgenetic interaction profilesgenetic interactionsperinuclear condensatephysical interactions

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Area of Science:

  • Cellular biology
  • Biochemistry
  • Systems biology

Background:

  • Molecular chaperones are essential for protein homeostasis, assisting in protein folding and preventing aggregation.
  • Understanding the complex network of chaperone interactions is crucial for deciphering cellular stress responses.

Purpose of the Study:

  • To comprehensively map the molecular chaperone interaction network in Saccharomyces cerevisiae.
  • To identify functional chaperone supercomplexes and their roles in cellular processes.

Main Methods:

  • Global integrative network analysis using physical and genetic interaction mapping.
  • In vitro reconstitution assays to study condensate formation.

Main Results:

  • Deciphered interactions for all core chaperones (67) and cochaperones (15).
  • Identified a large chaperone functional supercomplex, the naturally joined (NAJ) chaperone complex (including Hsp40, Hsp70, Hsp90, AAA+, CCT, small Hsps).
  • Demonstrated condensate formation for Rvb1 and Rvb2 AAA+ ATPases, linking them to Hsp90 and stress-induced protein foci.

Conclusions:

  • The study reveals a highly interconnected chaperone network, including a novel NAJ supercomplex.
  • Chaperone interactions with stress-induced protein condensates highlight their role in cellular stress management.
  • The findings distinguish between chaperones with broad and narrow substrate specificities, impacting protein homeostasis.