complex(p(FPLX:HSP90), p(HGNC:STUB1))

Components

• 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