Chaperonin containing TCP1 subunit 2 (CCT2)

Chaperonin containing TCP1 subunit 2 (CCT2) is a protein subunit of the eukaryotic cytosolic chaperonin complex known as TRiC or CCT, comprising eight distinct subunits (CCT1–CCT8) arranged in two back-to-back rings[1][2][3][4]. As part of this complex, CCT2 is essential for ATP-dependent folding of key client proteins, notably cytoskeletal proteins like actin and tubulin, and more broadly, for folding proteins involved in cell cycle regulation, proliferation, and cellular structure[1][2][4]. Beyond its chaperone activity, CCT2 can also act as a monomeric autophagy receptor in "aggrephagy," where it binds misfolded or aggregated proteins and facilitates their degradation via the autophagic pathway, which is relevant in the context of neurodegenerative diseases[2][3]. Elevated expression of CCT2 is found in several cancers, where it supports tumor cell proliferation and invasiveness, making it a candidate biomarker and therapeutic target[4]. Loss or mutation of CCT2 disrupts proteostasis and has been implicated in diseases such as Leber congenital amaurosis and various cancers[1][2][3][4][5]. No drugs currently approved directly target CCT2, but preclinical studies have tested inhibitors like CT20p in cancer models[4].

Other names

T-complex protein 1 subunit betaCCTBTCP-1-betaCctbCCT-betaChaperonin containing T-complex polypeptide 1 subunit 2HEL-S-100nPRO1633epididymis secretory sperm binding protein Li 100n99D8.1

Inhibition of chaperonin folding activity (e.g., CT20p disrupts CCT complex, inhibiting its cancer-related substrate folding)[4]