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T1  - Dynamic Interaction of USP14 with the Chaperone HSC70 Mediates Crosstalk between the Proteasome, ER Signaling, and Autophagy 
SN  -  /  
UR  - http://hdl.handle.net/10138/312783 
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A1  - Srinivasan, Vignesh; Bruelle, Celine; Scifo, Enzo; Pham, Dan Duc; Soliymani, Rabah; Lalowski, Maciej; Lindholm, Dan Bj 
A2  -  
PB  -  
Y1  - 2020 
LA  - eng 
AB  - USP14 is a deubiquitinating enzyme associated with the proteasome that is important for protein degradation. Here we show that upon proteasomal inhibition or expression of the mutant W58A38 USP14, association of USP14 with the 19S regulatory particle is disrupted. MS-based interactomics revealed an interaction of USP14 with the chaperone, HSC70 in neuroblastoma cells. Proteasome inhibition enhanced binding of USP14 to HSC70, but also to XBP1u and IRE1α proteins, demonstrating a role in the unfol... 
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IS  -  
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OP  -  
KW  - 1182 Biochemistry, cell and molecular biology; USP14; HSC70; autophagy; ER stress; proteasome; Huntington's disease; DEUBIQUITINATING ENZYME USP14; PROTEIN; PROTEOMICS; REVEALS; BINDING; STRESS; KINASE; CELLS 
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PP  -  
ER  -