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

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.

• Fecha de publicación: 2013
• Institución: Universidad del Rosario
• Repositorio: Repositorio EdocUR - U. Rosario
• Idioma: eng
• OAI Identifier: oai:repository.urosario.edu.co:10336/23513
• Acceso en línea: https://doi.org/10.1016/j.bbrc.2013.02.094; https://repository.urosario.edu.co/handle/10336/23513
• Palabra clave: 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; 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; Western; Blotting
• License: Abierto (Texto Completo)