Involvement of T-complex protein 1-ring complex/chaperonin containing T-complex protein 1 (TRiC/CCT) in retrograde axonal transport through tau phosphorylation

The cytosolic chaperonin T-complex protein 1-ring complex (TRiC) or chaperonin containing T-complex protein 1 (CCT) is essential in de novo folding of approximately 10% of the eukaryotic, newly translated polypeptides as well as misfolded proteins. There is a close link between the TRiC/CCT cytosolic chaperonin and neurodegenerative diseases (Lopez et al., 2015). A lot of research suggests that CCT plays neuroprotective roles in neurodegenerative diseases including Huntington’s disease (Lopez et al., 2015). Either overexpression of a single or all eight subunits (CCT1-8) or treatment of the substrate-binding apical domain of yeast CCT1 (ApiCCT1) prevented mutant Huntingtin aggregation and improved cellular and neuronal functions (Zhao et al., 2016). Importantly, our recent study has demonstrated that both CCT and ApiCCT could reduce mutant Huntingtin level and enhance both anterograde and retrograde axonal transport of brain-derived neurotrophic factor. These results led to restoration of the trophic status of striatal neurons from a bacterial artificial chromosome transgenic mouse model of Huntington’s disease (Zhao et al., 2016)