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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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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.
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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...
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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.
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Updated: Sep 12, 2025

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Structural analyses define the molecular basis of clusterin chaperone function.

Patricia Yuste-Checa1,2, Alonso I Carvajal3, Chenchen Mi3

  • 1Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany. yuste@biochem.mpg.de.

Nature Structural & Molecular Biology
|August 8, 2025
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Summary
This summary is machine-generated.

Clusterin, a protein linked to Alzheimer's disease, uses unique peptide tails to prevent protein aggregation and aid cellular clearance. These tails enable its diverse roles in maintaining protein health and cell function.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Clusterin (apolipoprotein J) is a glycoprotein involved in extracellular proteostasis.
  • Its dysregulation is associated with late-onset Alzheimer disease.
  • The precise mechanism of clusterin function remained unclear.

Purpose of the Study:

  • To elucidate the structural basis of human clusterin function.
  • To understand how clusterin mediates its diverse roles in protein aggregation suppression and cellular uptake.

Main Methods:

  • X-ray crystallography to determine human clusterin structure.
  • Structure-based mutational analysis to assess peptide tail function.

Main Results:

  • Human clusterin exhibits a discontinuous three-domain architecture.
  • Disordered, hydrophobic peptide tails were identified as key functional elements.
  • These tails mediate chaperone activity against amyloid-β, tau, and α-synuclein aggregation.
  • The tails facilitate receptor binding, cellular uptake, and lipoprotein formation.
  • Tails remain accessible for chaperone function within lipoprotein complexes.

Conclusions:

  • Clusterin's versatile peptide tails are crucial for its chaperone activity and interaction with cellular machinery.
  • Clusterin maintains extracellular protein solubility and promotes clearance via endocytosis and lysosomal degradation.
  • These findings provide mechanistic insights into clusterin's role in proteostasis and neurodegenerative diseases.