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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in 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...

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Post-Translational Modification as an Allosteric Switch in Hsp90: How Dual Phosphorylation Locks Chaperone Complexes

Giorgio Bonollo1, Benedetto Roncati1, Luca Torielli1

  • 1Department of Chemistry, University of Pavia, Via Taramelli 12, 27100, Pavia, Italy.

The Journal of Physical Chemistry Letters
|July 6, 2026
PubMed
Summary

Dual phosphorylation of heat shock protein 90 beta (Hsp90β) acts as a molecular clamp. This stabilizes interactions crucial for epichaperome formation, offering therapeutic targets for diseases.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Heat shock protein 90 beta (Hsp90β) is a crucial molecular chaperone.
  • Post-translational modifications regulate Hsp90β function and client interactions.
  • Hsp90β plays a role in disease pathogenesis and is a therapeutic target.

Purpose of the Study:

  • To elucidate the atomistic mechanism of Hsp90β regulation by dual phosphorylation at Ser226/Ser255.
  • To understand how these modifications stabilize Hsp90β interaction states.
  • To explore the implications for epichaperome formation and disease biology.

Main Methods:

  • Multimicrosecond molecular dynamics (MD) simulations were employed.
  • Analysis focused on structural rigidity and allosteric communication within Hsp90β.
  • Investigated the stabilization of cochaperone-client interfaces.

Main Results:

  • Dual phosphorylation at Ser226/Ser255 acts as a molecular clamp, rigidifying Hsp90β.
  • Phosphorylation propagates allosteric changes to distal domains.
  • Stabilization of cochaperone-client interfaces promotes epichaperome formation.

Conclusions:

  • Post-translational modifications like dual phosphorylation are key regulators of Hsp90β.
  • Provides an atomistic understanding of Hsp90β stabilization for epichaperome formation.
  • Highlights Hsp90β phosphorylation as a potential therapeutic strategy for diseases.