Ítem
Solo Metadatos
An N-terminal SIAH-interacting motif regulates the stability of the ubiquitin specific protease (USP)-19
Título de la revista
Autores
Velasco, Kelly
Zhao, Bin
Callegari, Simone
Altun, Mikael
Liu, Haiyin
Hassink, Gerco
Masucci, Maria G.
Lindsten, Kristina
Resumen
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. © 2013 Elsevier Inc.
Palabras clave
Keywords
Seven In Absentia Homolog 1 , Seven In Absentia Homolog 2 , Ubiquitin , Ubiquitin specific protease 19 , Unclassified drug , Amino terminal sequence , Article , Human , Human cell , Priority journal , Protein protein interaction , Protein stability , Ubiquitination , Unfolded protein response , Amino Acid Motifs , Blotting , Computational Biology , Endopeptidases , Enzyme Stability , HEK293 Cells , Hela Cells , Humans , Immunoprecipitation , Nuclear Proteins , Proteasome Endopeptidase Complex , Protein Binding , Protein Interaction Mapping , Proteolysis , Two-Hybrid System Techniques , Ubiquitin-Protein Ligases , Ubiquitination , Proteasomal degradation , SIAH degron , SIAH1 ligase , USP19
