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Inactive USP14 and inactive UCHL5 cause accumulation of distinct ubiquitinated proteins in mammalian cells

PLoS One.. 2019; 
Chadchankar J1, Korboukh V2, Conway LC1, Wobst HJ3, Walker CA3, Doig P2, Jacobsen SJ3, Brandon NJ3, Moss SJ3,4,5, Wang Q3.
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Mutant Libraries … Plasmids for tau (4R/2N), α-synuclein, USP14 and UCHL5 were purchased from Origene.<br> Mutant plasmids USP14 C114A, USP14 WT ΔUBL, USP14 C114A ΔUBL and UCHL5<br> C88A were generated from the wildtype plasmid by <b>Genscript</b> … Get A Quote

摘要

USP14 is a cysteine protease deubiquitinase associated with the proteasome and plays important catalytic and allosteric roles in proteasomal degradation. USP14 inhibition has been considered a therapeutic strategy for accelerating degradation of aggregation-prone proteins in neurodegenerative diseases and for inhibiting proteasome function to induce apoptotic cell death in cancers. Here we studied the effects of USP14 inhibition in mammalian cells using small molecule inhibitors and an inactive USP14 mutant C114A. Neither the inhibitors nor USP14 C114A showed consistent or significant effects on the level of TDP-43, tau or α-synuclein in HEK293T cells. However, USP14 C114A led to a robust accumulation of ubiqu... More

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