Inhibition of proteasome deubiquitinating activity as a new cancer therapy View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2011-12

AUTHORS

Pádraig D'Arcy, Slavica Brnjic, Maria Hägg Olofsson, Mårten Fryknäs, Kristina Lindsten, Michelandrea De Cesare, Paola Perego, Behnam Sadeghi, Moustapha Hassan, Rolf Larsson, Stig Linder

ABSTRACT

Ubiquitin-tagged substrates are degraded by the 26S proteasome, which is a multisubunit complex comprising a proteolytic 20S core particle capped by 19S regulatory particles. The approval of bortezomib for the treatment of multiple myeloma validated the 20S core particle as an anticancer drug target. Here we describe the small molecule b-AP15 as a previously unidentified class of proteasome inhibitor that abrogates the deubiquitinating activity of the 19S regulatory particle. b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCHL5) and ubiquitin-specific peptidase 14 (USP14), resulting in accumulation of polyubiquitin. b-AP15 induced tumor cell apoptosis that was insensitive to TP53 status and overexpression of the apoptosis inhibitor BCL2. We show that treatment with b-AP15 inhibited tumor progression in four different in vivo solid tumor models and inhibited organ infiltration in an acute myeloid leukemia model. Our results show that the deubiquitinating activity of the 19S regulatory particle is a new anticancer drug target. More... »

PAGES

1636

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nm.2536

DOI

http://dx.doi.org/10.1038/nm.2536

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1003070665

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/22057347


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