complex(p(FPLX:HSP90), p(HGNC:STUB1))
CHIP binds Hsp90 and Hsp70 with similar affinities and can regulate the degradation of chaperone clients (Kundrat and Regan, 2010). PubMed:25036637
Interestingly, it was recently found that reducing the levels of Akt, another client of the Hsp90/CHIP complex, facilitates tau degradation [123], suggesting a synchronized balance between competing Hsp90 substrates that may be driven, in part, by their relative abundance or susceptibility to Hsp90 binding PubMed:21882945
The co-chaperone CHIP interacts with Hsp70/Hsp90 to bind unfolded and misfolded proteins PubMed:25374103
Interestingly, it was recently found that reducing the levels of Akt, another client of the Hsp90/CHIP complex, facilitates tau degradation [123], suggesting a synchronized balance between competing Hsp90 substrates that may be driven, in part, by their relative abundance or susceptibility to Hsp90 binding PubMed:21882945
The co-chaperone CHIP interacts with Hsp70/Hsp90 to bind unfolded and misfolded proteins PubMed:25374103
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.