Cell type specific heat-shock-protein responses to bronchial thermoplasty in severe asthma treatment

Author(s):  
Lei Fang ◽  
Michael Tamm ◽  
Michael Roth ◽  
Daiana Stolz
2020 ◽  
Author(s):  
Huafeng Xu

AbstractThe molecular chaperone 90-kDa heat-shock protein (Hsp90) assists the late-stage folding and activation of diverse types of protein substrates (called clients), including many kinases. Previous studies have established that the Hsp90 homodimer undergoes an ATP-driven cycle through open and closed conformations. Here I propose a model of client activation by Hsp90, which predicts that this cycle enables Hsp90 to use ATP energy to drive a client out of thermodynamic equilibrium toward its active conformation. My model assumes that an Hsp90-bound client can transition between a deactivating conformation and an activating conformation. It suggests that the cochaperone Cdc37 aids Hsp90 to activate kinase clients by differentiating between these two intermediate conformations. My model makes experimentally testable predictions, including how modulating the stepwise kinetics of the Hsp90 cycle—for example, by various cochaperones—affects the activation of different clients. My model may inform client-specific and cell-type-specific therapeutic intervention of Hsp90-mediated protein activation.


Cancer ◽  
2010 ◽  
Vol 116 (16) ◽  
pp. 3785-3796 ◽  
Author(s):  
Manoj Garg ◽  
Deepika Kanojia ◽  
Shikha Saini ◽  
Sushma Suri ◽  
Anju Gupta ◽  
...  

1988 ◽  
Vol 103 (1) ◽  
pp. 81-85 ◽  
Author(s):  
Ken-ichi Honda ◽  
Takumi Hatayama ◽  
Munehiko Yukioka

1989 ◽  
Vol 160 (1) ◽  
pp. 60-66 ◽  
Author(s):  
Ken-ichi Honda ◽  
Takumi Hatayama ◽  
Munehiko Yukioka

2001 ◽  
Vol 432 (4) ◽  
pp. 425-439 ◽  
Author(s):  
Virginian McMillan Carr ◽  
Bert Ph.M. Menco ◽  
Maya P. Yankova ◽  
Richard I. Morimoto ◽  
Albert I. Farbman

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