T-complex protein 1 subunit delta (CCT4)

T-complex protein 1 subunit delta (CCT4) is one of the eight distinct subunits that compose the eukaryotic chaperonin-containing TCP1 complex (also known as TRiC or CCT), a molecular chaperone complex essential for ATP-dependent folding of newly synthesized proteins such as actin and tubulin[1][2][5]. CCT4 helps maintain cellular proteostasis and architecture by promoting efficient protein folding, and forms part of large oligomeric double-ring structures, either as a hetero-oligomer within the CCT complex or as homo-oligomers capable of chaperone activity[1][5]. Beyond general protein quality control, CCT4 is linked to specific pathophysiological contexts including neurodegeneration and several cancer types, where altered expression or function contributes to disease mechanisms (notably, promoting tumor growth via mTOR pathway activation in glioblastoma)[1]. Targeting CCT4 pharmacologically is considered challenging due to the fundamental nature of its biological role.

Other names

Chaperonin containing TCP1 subunit 4CCTDSRBTCP-1-deltaCctdCCT-deltaStimulator of TAR RNA-bindingCCT-DELTAChaperonin containing T-complex polypeptide 1 subunit 4chaperonin containing TCP1, subunit 4 (delta)chaperonin containing t-complex polypeptide 1, delta subunit

Modulation of protein folding capacity Potential modulation of mTOR pathway activity via involvement in chaperoning mLST8 in glioblastoma