Chaperonin containing TCP1 subunit 7 (CCT7)

Chaperonin containing TCP1 subunit 7 (CCT7) is a molecular chaperone and an integral member of the hetero-oligomeric TCP-1 ring complex (TRiC/CCT), which consists of two stacked rings of eight distinct subunits each. This complex mediates the ATP-dependent folding of newly synthesized polypeptides—most notably cytoskeletal actin and tubulin—as well as proteins involved in cell signaling, gene regulation, and chromatin remodeling. CCT7 interacts early in the conformational cycle of TRiC, initiating ring closure and facilitating proper polypeptide folding. Beyond its canonical role in proteostasis, CCT7 interacts with signaling Gβ subunits, assists G protein–coupled receptor biogenesis, and modulates epigenetic gene repression through chromatin association. Aberrant expression is associated with cancer, particularly hepatocellular carcinoma, and may play a role in neurodegenerative disease via impact on autophagy and protein aggregation. No current drugs directly target CCT7, but its biological importance makes it a relevant area for future therapeutic research.

Other names

T-complex protein 1 subunit etaTCP-1-etaCCT-etaNIP7-1HIV-1 Nef-interacting proteinCCTHCCTETA

As CCT7 itself is not currently a direct drug target, mechanisms would generally include modulation of protein folding, alteration of actin/tubulin assembly, or inhibition/activation of chaperonin activity but no specific drugs or mechanisms are documented in results.