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TOPORS, a dual E3 ubiquitin and Sumo1 ligase, interacts with 26 S protease regulatory subunit 4, encoded by the PSMC1 gene

Opened Access TOPORS, a dual E3 ubiquitin and Sumo1 ligase, interacts with 26 S protease regulatory subunit 4, encoded by the PSMC1 gene

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Autor: Czub, Barbara
Shah, Amna Z.
Alfano, Giovanna
Kruczek, P.M.
Chakarova, Christina
Bhattacharya, Shom Shanker
Fecha: 2016
Publicado en: PLoS ONE, 11, 1-20.
Tipo de documento: Artículo
Resumen: The significance of the ubiquitin-proteasome system (UPS) for protein degradation has been highlighted in the context of neurodegenerative diseases, including retinal dystrophies. TOPORS, a dual E3 ubiquitin and SUMO1 ligase, forms a component of the UPS and selected substrates for its enzymatic activities, such as DJ-1/PARK7 and APOBEC2, are important for neuronal as well as retinal homeostasis, respectively. TOPORS is ubiquitously expressed, yet its mutations are only known to result in autosomal dominant retinitis pigmentosa. We performed a yeast two-hybrid (Y2H) screen of a human retinal cDNA library in order to identify interacting protein partners of TOPORS from the retina, and thus begin delineating the putative disease mechanism(s) associated with the retina-specific phenotype resulting from mutations in TOPORS. The screen led to isolation of the 26 S protease regulatory subunit 4 (P26s4/ PSMC1), an ATPase indispensable for correct functioning of UPS-mediated proteo...
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Cita: Czub, B., Shah, A.Z., Alfano, G., Kruczek, P.M., Chakarova, C. y Bhattacharya, S.S. (2016). TOPORS, a dual E3 ubiquitin and Sumo1 ligase, interacts with 26 S protease regulatory subunit 4, encoded by the PSMC1 gene. PLoS ONE, 11, 1-20.
Tamaño: 2.847Mb
Formato: PDF

URI: https://hdl.handle.net/11441/81477

DOI: 10.1371/journal.pone.0148678

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