| First Author | Oftedal BE | Year | 2021 |
| Journal | Commun Biol | Volume | 4 |
| Issue | 1 | Pages | 681 |
| PubMed ID | 34083746 | Mgi Jnum | J:308345 |
| Mgi Id | MGI:6725243 | Doi | 10.1038/s42003-021-02203-0 |
| Citation | Oftedal BE, et al. (2021) The chaperonin CCT8 controls proteostasis essential for T cell maturation, selection, and function. Commun Biol 4(1):681 |
| abstractText | T cells rely for their development and function on the correct folding and turnover of proteins generated in response to a broad range of molecular cues. In the absence of the eukaryotic type II chaperonin complex, CCT, T cell activation induced changes in the proteome are compromised including the formation of nuclear actin filaments and the formation of a normal cell stress response. Consequently, thymocyte maturation and selection, and T cell homeostatic maintenance and receptor-mediated activation are severely impaired. In the absence of CCT-controlled protein folding, Th2 polarization diverges from normal differentiation with paradoxical continued IFN-gamma expression. As a result, CCT-deficient T cells fail to generate an efficient immune protection against helminths as they are unable to sustain a coordinated recruitment of the innate and adaptive immune systems. These findings thus demonstrate that normal T cell biology is critically dependent on CCT-controlled proteostasis and that its absence is incompatible with protective immunity. |
