An N-terminal SIAH-interacting motif regulates the stability of the ubiquitin specific protease (USP)-19

Kelly Velasco, Bin Zhao, Simone Callegari, Mikael Altun, Haiyin Liu, Gerco Hassink, Maria G. Masucci*, Kristina Lindsten*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

12 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)390-395
Number of pages6
JournalBiochemical and biophysical research communications
Volume433
Issue number4
Early online date13 Mar 2013
DOIs
Publication statusPublished - 19 Apr 2013
Externally publishedYes

Keywords

  • Proteasomal degradation
  • SIAH degron
  • SIAH1 ligase
  • USP19

Fingerprint

Dive into the research topics of 'An N-terminal SIAH-interacting motif regulates the stability of the ubiquitin specific protease (USP)-19'. Together they form a unique fingerprint.

Cite this