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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

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.
The...
Molecular Chaperones and Protein Folding03:00

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.
The...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
The Spindle Assembly Checkpoint02:19

The Spindle Assembly Checkpoint

The spindle assembly checkpoint is a molecular surveillance mechanism ensuring the fidelity of chromosome segregation during anaphase. The checkpoint monitors the completion of all the prerequisite steps before chromosome segregation to determine whether the segregation process should proceed or be delayed.
Many proteins function together to control the spindle assembly checkpoint. Mutations affecting these proteins may allow cells to proceed into anaphase prematurely, resulting in the...
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...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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...

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Related Experiment Video

Updated: May 9, 2026

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: chaperone-me-not.

J M Patki1, S S Pawar

  • 1Department of Biotechnology and Bioinformatics, Padmashree Dr D.Y. Patil University, Sector-15, Plot-50, CBD Belapur, Navi Mumbai, India, jyotitope8@gmail.com.

Pathology Oncology Research : POR
|August 1, 2013
PubMed
Summary
This summary is machine-generated.

Heat shock protein 90 (Hsp90) is crucial for cancer cell survival and proliferation. Inhibiting Hsp90 offers a promising therapeutic strategy, selectively targeting cancer cells by disrupting multiple oncogenic pathways.

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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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Intracellular Refolding Assay
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Intracellular Refolding Assay

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Last Updated: May 9, 2026

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

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Published on: July 21, 2021

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

Intracellular Refolding Assay
07:18

Intracellular Refolding Assay

Published on: January 24, 2012

Area of Science:

  • Molecular Biology
  • Oncology
  • Biochemistry

Background:

  • Cancer therapy is evolving towards targeted molecular approaches based on understanding carcinogenesis.
  • Key proteins regulating cell survival, proliferation, and apoptosis are essential for malignant transformation.
  • Heat shock protein 90 (Hsp90) is a molecular chaperone vital for the folding, stability, and function of these cancer-associated proteins.

Purpose of the Study:

  • To review the role of Hsp90 in cancer.
  • To discuss the tumor selectivity of Hsp90 inhibitors.
  • To present the current status of Hsp90 inhibitors in cancer therapeutics.

Main Methods:

  • Literature review of Hsp90's role in cancer.
  • Analysis of Hsp90 client proteins and their dependence on the chaperone.
  • Examination of Hsp90 inhibitor development and clinical status.

Main Results:

  • Hsp90 client proteins are integral to multiple oncogenic signaling pathways.
  • Hsp90 inhibition affects numerous cancer-driving pathways simultaneously.
  • Hsp90 inhibitors demonstrate selective toxicity towards cancer cells over normal cells.
  • Cancer cells exhibit a heightened dependence on Hsp90 for maintaining protein homeostasis.

Conclusions:

  • Hsp90 is a critical regulator of cancer cell viability and a validated therapeutic target.
  • Targeting Hsp90 offers a strategy for simultaneously disrupting multiple oncogenic pathways.
  • Hsp90 inhibitors represent a promising class of anti-cancer drugs with demonstrated tumor selectivity.