Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10759565 | Biochemical and Biophysical Research Communications | 2013 | 6 Pages |
Abstract
The Ubiquitin Specific Protease-19 (USP19) regulates cell cycle progression and is involved in the cellular response to different types of stress, including the unfolded protein response (UPR), hypoxia and muscle atrophy. Using the unique N-terminal domain as bait in a yeast-two hybrid screen we have identified the ubiquitin ligases Seven In Absentia Homolog (SIAH)-1 and SIAH2 as binding partners of USP19. The interaction is mediated by a SIAH-consensus binding motif and promotes USP19 ubiquitylation and proteasome-dependent degradation. These findings identify USP19 as a common substrate of the SIAH ubiquitin ligases.
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Authors
Kelly Velasco, Bin Zhao, Simone Callegari, Mikael Altun, Haiyin Liu, Gerco Hassink, Maria G. Masucci, Kristina Lindsten,