p(FPLX:"CCT_complex")
TRiC is essential for proper posttranslational folding of the cytoskeletal components actin and tubulin and is therefore essential for cell structure, division, and cargo delivery (11). PubMed:25784053
HSF1A suppresses toxicity in cell and tissue culture models of HD and SCA-3/MJD and appears to activate HSF1 by impairing the activity of TRiC, a recently discovered negative regulator of HSF1. PubMed:25784053
TRiC is essential for proper posttranslational folding of the cytoskeletal components actin and tubulin and is therefore essential for cell structure, division, and cargo delivery (11). PubMed:25784053
TRiC is essential for proper posttranslational folding of the cytoskeletal components actin and tubulin and is therefore essential for cell structure, division, and cargo delivery (11). PubMed:25784053
This functional screen identified 18 genes (Figure 3D), corresponding to ten ATP-dependent chaperones, HSC70 (hsp-1), HSP90 (daf-21), and eight subunits of the CCT/TRiC chaperonin complex; the co-chaperones, HSP40 (dnj-12) and CDC37 (cdc-37); and the TPR-domain pro- tein STI1 that upon knockdown significantly enhanced A b 42 pro- teotoxicity (Figure 3D). PubMed:25437566
These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566
TRiC is essential for proper posttranslational folding of the cytoskeletal components actin and tubulin and is therefore essential for cell structure, division, and cargo delivery (11). PubMed:25784053
TRiC is essential for proper posttranslational folding of the cytoskeletal components actin and tubulin and is therefore essential for cell structure, division, and cargo delivery (11). PubMed:25784053
TRiC is essential for proper posttranslational folding of the cytoskeletal components actin and tubulin and is therefore essential for cell structure, division, and cargo delivery (11). PubMed:25784053
HSF1A suppresses toxicity in cell and tissue culture models of HD and SCA-3/MJD and appears to activate HSF1 by impairing the activity of TRiC, a recently discovered negative regulator of HSF1. PubMed:25784053
TRiC also interacts with N-terminal fragments of mutant huntingtin that contain an expanded polyglutamine repeat sequence (165–168). Binding to TRiC modulates the aggregation properties of this protein and reduces its cytotoxicity. PubMed:23746257
BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.
If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.