4.8 Editorial Material

CCT2, a newly identified aggrephagy receptor in mammals, specifically mediates the autophagic clearance of solid protein aggregates

Journal

AUTOPHAGY
Volume 18, Issue 7, Pages 1483-1485

Publisher

TAYLOR & FRANCIS INC
DOI: 10.1080/15548627.2022.2083305

Keywords

Aggrephagy; autophagy; CCT2; chaperonin TRiC subunit; protein aggregation; solid protein aggregates

Categories

Funding

  1. National Institute of General Medical Sciences [GM131919]

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Protein aggregates are closely related to the pathogenesis of various human diseases. A recent study identified CCT2 as a specific aggrephagy receptor in mammals, which plays a role in the autophagic clearance of protein aggregates. This finding suggests that CCT2 could be an important target for treating protein aggregation-related diseases.
Protein aggregates have a strong correlation with the pathogenesis of multiple human pathologies represented by neurodegenerative diseases. One type of selective autophagy, known as aggrephagy, can selectively degrade protein aggregates. A recent study from Ge lab reported the TRiC subunit CCT2 (chaperonin containing TCP1 subunit 2) as the first identified specific aggrephagy receptor in mammals. The switch of CCT2's role from a chaperonin to a specific aggrephagy receptor is achieved by CCT2 monomer formation. CCT2 functions independently of ubiquitin and the TRiC complex to facilitate the autophagic clearance of solid protein aggregates. This study provides the intriguing possibility that CCT2, as a specific aggrephagy receptor, might be an important target for the treatment of various diseases associated with protein aggregation.

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