Ontology highlight
ABSTRACT:
SUBMITTER: Woodford MR
PROVIDER: S-EPMC5730846 | biostudies-other | 2017 Dec
REPOSITORIES: biostudies-other
Woodford Mark R MR Sager Rebecca A RA Marris Elijah E Dunn Diana M DM Blanden Adam R AR Murphy Ryan L RL Rensing Nicholas N Shapiro Oleg O Panaretou Barry B Prodromou Chrisostomos C Loh Stewart N SN Gutmann David H DH Bourboulia Dimitra D Bratslavsky Gennady G Wong Michael M Mollapour Mehdi M
The EMBO journal 20171110 24
The tumor suppressors Tsc1 and Tsc2 form the tuberous sclerosis complex (TSC), a regulator of mTOR activity. Tsc1 stabilizes Tsc2; however, the precise mechanism involved remains elusive. The molecular chaperone heat-shock protein 90 (Hsp90) is an essential component of the cellular homeostatic machinery in eukaryotes. Here, we show that Tsc1 is a new co-chaperone for Hsp90 that inhibits its ATPase activity. The C-terminal domain of Tsc1 (998-1,164 aa) forms a homodimer and binds to both protome ...[more]