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Related Concept Videos

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...
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...
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...
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...
Protein Complex Assembly02:41

Protein 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...

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

Published on: July 21, 2021

Hsp90 and client protein maturation.

Natalie Wayne1, Parul Mishra, Daniel N Bolon

  • 1Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|September 8, 2011
PubMed
Summary
This summary is machine-generated.

Heat-shock protein 90 (Hsp90) is a crucial molecular chaperone. Its clients, involved in cancer and cystic fibrosis, drive intensified research into Hsp90

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Last Updated: May 29, 2026

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
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Published on: July 21, 2021

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
07:57

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Biochemical Reconstitution of Steroid Receptor&#x2022;Hsp90 Protein Complexes and Reactivation of Ligand Binding
11:07

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding

Published on: September 21, 2011

Area of Science:

  • Molecular biology
  • Cellular biology
  • Biochemistry

Background:

  • Heat-shock protein 90 (Hsp90) acts as a molecular chaperone.
  • Hsp90 facilitates the maturation of specific substrate proteins, known as clients.
  • Many Hsp90 clients are key players in signal transduction pathways, including kinases and steroid hormone receptors.

Purpose of the Study:

  • To review the historical progression of Heat-shock protein 90 (Hsp90) research.
  • To categorize Hsp90 clients into distinct functional groups: kinases, hormone receptors, and non-signal transduction proteins.
  • To highlight current and active areas of Hsp90 investigation.

Main Methods:

  • Literature review of Hsp90 research.
  • Classification of Hsp90 client proteins based on their functions.
  • Analysis of Hsp90's role in signal transduction and non-signal transduction pathways.

Main Results:

  • Hsp90 client proteins are broadly categorized into signal transduction (kinases, hormone receptors) and non-signal transduction groups (telomerase, CFTR, antigenic peptides).
  • Hsp90 clients are implicated in significant diseases such as cancer and cystic fibrosis.
  • Research on Hsp90 has significantly increased due to its clients' roles in disease.

Conclusions:

  • Hsp90's diverse client portfolio underscores its importance in cellular function.
  • Understanding Hsp90-client interactions is critical for developing therapeutic strategies for cancer and cystic fibrosis.
  • Continued research into Hsp90 and its clients will likely yield further insights into disease mechanisms and potential treatments.