T-complex protein 1 subunit zeta-2 (CCT6B)

T-complex protein 1 subunit zeta-2 (CCT6B) is a molecular chaperone and a component of the chaperonin-containing TCP1 complex (also called TRiC). This complex consists of two rings, each with eight unique subunits, which function collaboratively to fold newly synthesized polypeptides such as actin and tubulin in an ATP-dependent manner. CCT6B is expressed in various tissues, including testis, and plays a role in protein folding, cytoskeletal organization, and potentially tissue-specific processes. While most CCT subunits are overexpressed in several cancers and linked to poor prognosis, CCT6B paradoxically shows reduced expression in hepatocellular carcinoma, and higher levels predict better patient survival, highlighting a unique role among chaperonin subunits[1][2][3].

Other names

CCT6BChaperonin containing TCP1 subunit 6BTCP-1-zeta-2Cctz2TSA303CCT-zeta-2CCTZ-2TCP-1-zeta-likeTestis-specific Tcp20Testis-specific protein TSA303CCT-zeta-likeChaperonin-containing T-complex polypeptide 1 subunit 6BT-complex protein 1 subunit zeta-2

No specific drugs directly targeting CCT6B; mechanism would theoretically be modulation of protein folding or chaperone activity.