Chaperonin-containing TCP-1 complex (CCT)

The Chaperonin-containing TCP-1 complex (CCT), also known as the TCP-1 ring complex (TRiC), is a large, 1-megadalton hetero-oligomeric protein complex essential for protein folding in the eukaryotic cytosol (UniProt, 2024). It consists of two back-to-back rings, each composed of eight distinct subunits (CCT1-CCT8), which form a central cavity where substrate proteins fold in an ATP-dependent manner (Nature Reviews Molecular Cell Biology, 2011). CCT is uniquely responsible for folding approximately 10% of the proteome, including critical proteins such as actin, tubulin, and various cell cycle regulators like CDC20 (PubMed, 2020). Because many of its substrates are essential for cell proliferation and signaling, CCT is frequently overexpressed in various cancers, where it supports the high demand for protein synthesis and folding (Frontiers in Oncology, 2020). Consequently, CCT has emerged as a promising therapeutic target, with research focusing on small molecules and peptides like CT20p that can inhibit its folding activity or disrupt its assembly to induce proteotoxic stress and apoptosis in malignant cells (Cell Death & Disease, 2014).

Other names

TCP-1 ring complexTRiCCCT complexChaperonin containing T-complex polypeptide 1

Inhibition of the ATP-dependent protein folding cycle and disruption of substrate binding (e.g., actin and tubulin).