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Aggregate fragmentation: the ticket to aggrephagy.

Mario Mauthe1, Harm Kampinga1, Fulvio Reggiori2

  • 1Department of Biomedical Sciences, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.

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|September 17, 2025
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Summary
This summary is machine-generated.

Protein aggregate fragmentation is essential for aggrephagy, the clearance of amorphous aggregates. This process requires a chaperone module and proteasome components to fragment and compact aggregates for autophagic removal.

Keywords:
Amorphousamyloidchaperoneclusteringproteasomeselective autophagy receptors

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Protein aggregates are implicated in various neurodegenerative diseases.
  • Autophagy is a key cellular process for clearing damaged components, including protein aggregates.
  • Aggrephagy is a specialized form of autophagy targeting protein aggregates.

Purpose of the Study:

  • To identify the molecular mechanisms underlying the clearance of amorphous protein aggregates via aggrephagy.
  • To elucidate the roles of chaperone proteins and the proteasome in aggregate fragmentation.
  • To investigate the fragmentase activity in the context of disease-related protein aggregates.

Main Methods:

  • Utilized biochemical assays to study protein aggregate fragmentation.
  • Investigated the involvement of chaperone modules (DNAJB6-HSPA/HSP70-HSPH1/HSP110) and proteasome 19S regulatory particles (RPs).
  • Examined the impact of fragmentation on selective autophagy receptor (SAR) clustering and phagophore formation.

Main Results:

  • Discovered a requirement for protein aggregate fragmentation prior to autophagic clearance (aggrephagy).
  • Demonstrated that aggregate fragmentation is mediated by a cooperative interaction between a specific chaperone module and proteasome RPs.
  • Showed that this fragmentation process also compacts aggregates, facilitating SAR clustering and phagophore formation.
  • Confirmed the role of this fragmentase activity in clearing various aggregate types, including disease-associated huntingtin (HTT) aggregates.

Conclusions:

  • Protein aggregate fragmentation is a critical, previously unrecognized step in aggrephagy.
  • The DNAJB6-HSPA/HSP70-HSPH1/HSP110 chaperone module and proteasome RPs cooperate to fragment and compact aggregates.
  • This mechanism is crucial for efficient aggrephagic clearance and has implications for diseases involving protein aggregation.