http://purl.uniprot.org/citations/24068323 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/24068323 | http://www.w3.org/2000/01/rdf-schema#comment | "Endoplasmic reticulum (ER) membrane-bound E3 ubiquitin ligases promote ER-associated degradation (ERAD) by ubiquitinating a retro-translocated substrate that reaches the cytosol from the ER, targeting it to the proteasome for destruction. Recent findings implicate ERAD-associated deubiquitinases (DUBs) as positive and negative regulators during ERAD, reflecting the different consequences of deubiquitinating a substrate prior to proteasomal degradation. These observations raise the question of whether a DUB can control the fate of a nonubiquitinated ERAD substrate. In this study, we probed the role of the ERAD-associated DUB, YOD1, during retro-translocation of the nonubiquitinated cholera toxin A1 (CTA1) peptide, a critical intoxication step. Through combining knockdown, overexpression, and binding studies, we demonstrated that YOD1 negatively controls CTA1 retro-translocation, likely by deubiquitinating and inactivating ubiquitinated ERAD components that normally promote toxin retro-translocation. YOD1 also antagonizes the proteasomal degradation of nonglycosylated pro-α factor, a postulated nonubiquitinated yeast ERAD substrate, in mammalian cells. Our findings reveal that a cytosolic DUB exerts a negative function during retro-translocation of nonubiquitinated substrates, potentially by acting on elements of the ERAD machinery."xsd:string |
http://purl.uniprot.org/citations/24068323 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.e13-06-0332"xsd:string |
http://purl.uniprot.org/citations/24068323 | http://purl.uniprot.org/core/author | "Inoue T."xsd:string |
http://purl.uniprot.org/citations/24068323 | http://purl.uniprot.org/core/author | "Schultz A."xsd:string |
http://purl.uniprot.org/citations/24068323 | http://purl.uniprot.org/core/author | "Williams J.M."xsd:string |
http://purl.uniprot.org/citations/24068323 | http://purl.uniprot.org/core/author | "Tsai B."xsd:string |
http://purl.uniprot.org/citations/24068323 | http://purl.uniprot.org/core/author | "Bernardi K.M."xsd:string |
http://purl.uniprot.org/citations/24068323 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
http://purl.uniprot.org/citations/24068323 | http://purl.uniprot.org/core/name | "Mol Biol Cell"xsd:string |
http://purl.uniprot.org/citations/24068323 | http://purl.uniprot.org/core/pages | "3545-3556"xsd:string |
http://purl.uniprot.org/citations/24068323 | http://purl.uniprot.org/core/title | "A deubiquitinase negatively regulates retro-translocation of nonubiquitinated substrates."xsd:string |
http://purl.uniprot.org/citations/24068323 | http://purl.uniprot.org/core/volume | "24"xsd:string |
http://purl.uniprot.org/citations/24068323 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24068323 |
http://purl.uniprot.org/citations/24068323 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/24068323 |
http://purl.uniprot.org/uniprot/P54252#attribution-A85C287F23BA78323F8F75D1343B8FFB | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/24068323 |
http://purl.uniprot.org/uniprot/Q5VVQ6#attribution-45C7947320AA0400751B591309CFE903 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/24068323 |
http://purl.uniprot.org/uniprot/Q5VVQ6#attribution-A85C287F23BA78323F8F75D1343B8FFB | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/24068323 |
http://purl.uniprot.org/uniprot/Q5VVQ6#attribution-F97B0CD389E30EBCFBBDDEFC7B6A245C | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/24068323 |
http://purl.uniprot.org/uniprot/Q86TM6#attribution-A85C287F23BA78323F8F75D1343B8FFB | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/24068323 |