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Related Concept Videos

Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Molecular 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.
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Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
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Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

HSP90 manages the ends.

Diane C DeZwaan1, Brian C Freeman

  • 1Department of Cell and Developmental Biology, University of Illinois, Urbana-Champaign, Urbana, IL 61801, USA.

Trends in Biochemical Sciences
|March 19, 2010
PubMed
Summary
This summary is machine-generated.

The HSP90 molecular chaperone network efficiently manages telomere structures, overcoming challenges like competitive DNA binding and cell cycle restrictions to maintain cellular homeostasis.

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Last Updated: Jun 15, 2026

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Area of Science:

  • Molecular biology
  • Cellular biology
  • Genetics

Background:

  • Telomeres require dynamic structural assembly and disassembly for cellular homeostasis.
  • Telomeric DNA binding proteins can compete, complicating interactions.
  • Cell cycle restrictions limit the time available for telomere maintenance tasks.

Purpose of the Study:

  • To review how the HSP90 molecular chaperone network facilitates telomere function.
  • To explain how HSP90 overcomes obstacles in the telomere environment.

Main Methods:

  • Literature review of studies on telomere biology and HSP90 function.

Main Results:

  • HSP90 network proteins exhibit specific binding properties that prevent competitive DNA interactions.
  • HSP90 facilitates timely and efficient management of telomeric structures within cell cycle constraints.

Conclusions:

  • The HSP90 molecular chaperone network is crucial for the effective operation of the telomere system.
  • HSP90's role in managing telomere structure ensures cellular homeostasis.