Also known as the Chaperonin Containing TCP-1 (CCT) or Tcp-1 Ring Complex (TRiC), the TCP-1 complex is an integral component of the Tubulin-folding pathway [ 3, 6, 7].
TNFα was firstly coupled with a vascular-homing peptide TCP-1 to form a TNFα derivative (TCP-1/TNFα).
The eukaryotic cytosolic chaperonin CCT (chaperonin-containing TCP-1) assists folding of newly synthesized polypeptides.
TCP-1 was first identified as a molecular chaperone for tubulin.
Multiple components of the chaperonin containing TCP-1 complex (CCT, also called TRiC) [22] were present in Slm9-FLAG purifications.
This chaperonin is predicted to be the theta subunit of the heterometric TCP-1 complex involved in protein folding [63].
BDNF transcriptional regulation of T-complex 1 (TCP-1) was also reversed by CMP treatment (reduction in CMP state, potentiation in control state).
In Sarcophaga crassipalpis, the expression of TCP-1, which encodes the α subunit of CCT, was upregulated by the entering of diapause [4].
TCP-1 β was expressed predominantly on renal tubules.
Similarly, it has been proposed that TCP-1 interacts with the proteasome and facilitates the degradation of TCP-1 substrates that have misfolded; the TCP-1 complex functions in assisting protein degradation through interaction with the proteasome.
But expression of TCP-1 β in renal tubules was so strong that TCP-1 β in mesangial glomerula was obscured.
