CCT2 (chaperonin containing TCP1 subunit 2) is a multifunctional protein that serves dual roles as both a molecular chaperone and an autophagy receptor. As a component of the TRiC chaperonin complex, CCT2 assists in the ATP-dependent folding of actin, tubulin, and other proteins, with assembly occurring through a hierarchical pathway where CCT2 forms part of the negatively charged hemisphere 1. Beyond its traditional chaperone function, CCT2 uniquely functions as an aggrephagy receptor for the selective clearance of solid protein aggregates 2. This dual functionality is achieved through a functional switch where aggregation-prone proteins induce CCT2 monomer formation, exposing a VLIR motif that enables interaction with ATG8 proteins, thereby promoting autophagic degradation independent of ubiquitination 2. The aggrephagy function is regulated by ATG1-mediated phosphorylation at Ser412 and Ser470, and interaction with ATG11 adaptor protein 3. Clinically, CCT2 has significant disease relevance, being overexpressed in multiple cancers including breast cancer, glioblastoma, and papillary thyroid carcinoma, where it promotes tumor progression through various mechanisms including KRAS stabilization and EMT regulation 456. The protein's role in clearing solid aggregates makes it a potential therapeutic target for neurodegenerative diseases and cancer treatment 7.