Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors
详细信息 查看全文
- 作者：Mark R. Woodford1 ; 2 ; 3 ; 12 ; Andrew W. Truman4 ; 12 ; Diana M. Dunn1 ; 2 ; 3 ; Sandra M. Jensen9 ; Richard Cotran1 ; 3 ; Renee Bullard1 ; 2 ; 3 ; Mourad Abouelleil1 ; 3 ; Kristin Beebe10 ; Donald Wolfgeher5 ; Sara Wierzbicki1 ; 3 ; Dawn E. Post1 ; 2 ; 3 ; Tiffany Caza6 ; Shinji Tsutsumi10 ; Barry Panaretou7 ; Stephen J. Kron5 ; Jane B. Trepel11 ; Steve Landas6 ; Chrisostomos Prodromou8 ; Oleg Shapiro1 ; 3 ; William G. Stetler-Stevenson9 ; Dimitra Bourboulia1 ; 2 ; 3 ; Len Neckers10 ; Gennady Bratslavsky1 ; 3 ; Mehdi Mollapour1 ; 2 ; 3 ; mollapom@upstate.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：heat shock protein-90 ; phosphorylation ; kinase ; phosphatase ; molecular chaperones ; mitotic checkpoint ; Mps1 ; Cdc14 ; renal cell carcinoma
- 刊名：Cell Reports
- 出版年：2016
- 出版时间：2 February 2016
- 年：2016
- 卷：14
- 期：4
- 页码：872-884
- 全文大小：4122 K
文摘
- •
Mps1 phosphorylates a conserved threonine in Hsp90 and regulates its function
- •
Hsp90 phosphorylation by Mps1 is essential for the mitotic checkpoint
- •
Cdc14 phosphatase dephosphorylates Hsp90 and disrupts the Mps1-Hsp90 complex
- •
Mps1 phosphorylation of Hsp90 confers tumor selectivity to its inhibitors