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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Amyloid Fibrils03:03

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Proteins: From Genes to Degradation02:11

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Related Experiment Video

Updated: May 15, 2026

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
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DNAJ proteins and protein aggregation diseases.

Vaishali Kakkar1, Louis C B Prins, Harm H Kampinga

  • 1University of Groningen, University Medical Center Groningen, Department of Cell Biology, Groningen, The Netherlands.

Current Topics in Medicinal Chemistry
|January 24, 2013
PubMed
Summary

Aging cells struggle with protein buildup due to declining chaperone networks. DNAJ proteins, crucial Hsp70 co-chaperones, are key to managing disease-related protein aggregation and cellular proteostasis.

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Area of Science:

  • Molecular biology
  • Cellular aging
  • Neurodegenerative disease research

Background:

  • Aging is linked to reduced chaperone function and increased damaged protein accumulation, impairing cellular protein homeostasis.
  • Neurodegenerative diseases often involve protein aggregation, suggesting aged cells are vulnerable to proteotoxic stress.
  • DNAJ proteins, as Hsp70 co-chaperones, are implicated as a potential rate-limiting factor in managing disease-associated proteins.

Purpose of the Study:

  • To review the role of DNAJ proteins in the aggregation of disease-causing proteins.
  • To investigate the dependence of DNAJ protein function on their role as Hsp70 co-chaperones and the specific disease-causing protein.
  • To discuss DNAJ chaperonopathies, degenerative diseases linked to mutations in DNAJ members.

Main Methods:

  • Literature review of studies on DNAJ proteins, Hsp70 machinery, and protein aggregation.
  • Analysis of the functional mechanisms of DNAJ proteins in cellular proteostasis.
  • Examination of genetic links between DNAJ mutations and specific neurodegenerative diseases.

Main Results:

  • DNAJ proteins significantly influence the aggregation of disease-associated proteins.
  • The impact of DNAJ proteins is modulated by their co-chaperone activity with Hsp70 and the nature of the aggregated protein.
  • Five distinct neurodegenerative diseases are associated with mutations in specific DNAJ proteins, highlighting their critical role.

Conclusions:

  • DNAJ proteins are central players in preventing or promoting protein aggregation, impacting neurodegenerative disease pathology.
  • Understanding DNAJ protein function and regulation is crucial for developing therapeutic strategies against age-related proteinopathies.
  • DNAJ chaperonopathies represent a class of diseases where defects in protein quality control mediated by DNAJ proteins lead to neurodegeneration.