Ontology highlight
ABSTRACT:
SUBMITTER: Li Z
PROVIDER: S-EPMC5489699 | biostudies-literature | 2017 Jun
REPOSITORIES: biostudies-literature
Li Zhaobo Z Zhou Lihong L Prodromou Chrisostomos C Savic Velibor V Pearl Laurence H LH
Cell reports 20170601 12
Inhibition of the ATPase cycle of the HSP90 chaperone promotes ubiquitylation and proteasomal degradation of its client proteins, which include many oncogenic protein kinases. This provides the rationale for HSP90 inhibitors as cancer therapeutics. However, the mechanism by which HSP90 ATPase inhibition triggers ubiquitylation is not understood, and the E3 ubiquitin ligases involved are largely unknown. Using a siRNA screen, we have identified components of two independent degradation pathways f ...[more]