CCT8
CCT8 (chaperonin containing TCP1 subunit 8, also known as T-complex protein 1 subunit theta, Cctq, PRED71 or C21orf112) is the theta subunit of the CCT chaperonin. It works within the TRiC complex to help fold actin, tubulin and other proteins. Browse Assay Genie's current range of CCT8 research reagents below, or read on for the biology behind the target.
CCT8 is a component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists protein folding upon ATP hydrolysis. Actin and tubulin are well-established substrates, along with other proteins. TRiC also mediates the folding of WRAP53/TCAB1, and through this it regulates telomere maintenance. As part of TRiC, CCT8 may also play a role in the assembly of the BBSome, a complex involved in ciliogenesis that regulates the transport of vesicles to the cilia.
The CCT8 gene encodes the theta subunit of the CCT chaperonin, which is abundant in the eukaryotic cytosol and may be involved in the transport and assembly of newly synthesised proteins. The protein belongs to the TCP-1 chaperonin family and is annotated with an EC number of 3.6.1.-, reflecting its ATP-hydrolysing activity. UniProt places it in the cytoplasm, at the centrosome within the microtubule organising centre, and at the cilium basal body. Alternative splicing produces multiple transcript variants, and a related pseudogene is located on chromosome 1. The mouse ortholog is Cct8.
HGNC classifies the gene in the chaperonin containing TCP1 group. Earlier names include chromosome 21 open reading frame 112 (C21orf112) and chaperonin containing TCP1, subunit 8 (theta), and PRED71 and Cctq remain in use as aliases. Researchers studying CCT8 typically work on chaperone-assisted folding, cytoskeletal protein biogenesis, telomere biology and ciliary assembly.
CCT8 is part of TRiC, which assists the ATP-dependent folding of actin, tubulin and other proteins in the cytosol.
TRiC mediates the folding of WRAP53/TCAB1, linking CCT8-containing chaperonin activity to the regulation of telomere maintenance.
As part of TRiC, CCT8 may contribute to BBSome assembly, a complex that regulates vesicle transport to the cilia.
CCT8 localises to the cytoplasm, centrosome and cilium basal body, making it relevant to studies of cytoskeletal protein folding and organisation.
CCT8 is a subunit of the TRiC chaperonin complex, which assists the folding of actin, tubulin and other proteins upon ATP hydrolysis. TRiC also mediates folding of WRAP53/TCAB1, thereby regulating telomere maintenance, and may help assemble the BBSome involved in ciliogenesis.
CCT8 is also called T-complex protein 1 subunit theta, Cctq, PRED71 and C21orf112. Previous HGNC names are chromosome 21 open reading frame 112 and chaperonin containing TCP1, subunit 8 (theta). Alternative splicing gives multiple transcript variants of the gene.
The mouse has an ortholog named Cct8, and the protein belongs to the TCP-1 chaperonin family. NCBI notes the CCT chaperonin is abundant in the eukaryotic cytosol. Check the datasheet of any product for its validated reactivity.
Other subunits of the TRiC chaperonin complex with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P50990; product specifications from Assay Genie datasheets.