| http://purl.uniprot.org/citations/36682332 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/36682332 | http://www.w3.org/2000/01/rdf-schema#comment | "α-synuclein is one of the proteins involved in degenerative neuronal diseases such as Parkinson's disease (PD) or Lewy body dementia (LBD). The pathogenesis is imparted by the abnormal accumulation of α-synuclein resulting in the formation of a Lewy body (LB) and exerting neurotoxicity via an unknown mechanism. Regulation of α-synuclein is achieved by the ubiquitin-proteasome system (UPS), which influences protein homeostasis via inducing proteasome-dependent degradation by attaching a small molecule (ubiquitin) to the substrate. Deubiquitinating enzymes (DUBs) control the UPS by cleaving the peptide or isopeptide bond between ubiquitin and its substrate proteins. In a previous study, we found that YOD1 deubiquitinates and regulates the cellular function of neural precursor cell expressed developmentally down-regulated protein 4 (NEDD4), an E3 ligase that induces α-synuclein degradation. We hypothesized that YOD1 acts as a DUB involved in a modulated pathway of α-synuclein. In the current study, we found that YOD1 directly interacts with α-synuclein and deubiquitinates K6-, K11-, K29-, K33-, and K63-linked polyubiquitin chains on α-synuclein. Furthermore, YOD1 destabilizes α-synuclein protein stability by upregulating NEDD4. Collectively, this suggests the possibility that YOD1 is potentially a new regulator in the NEDD4-α-synuclein pathway."xsd:string |
| http://purl.uniprot.org/citations/36682332 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2023.01.030"xsd:string |
| http://purl.uniprot.org/citations/36682332 | http://purl.uniprot.org/core/author | "Baek K.H."xsd:string |
| http://purl.uniprot.org/citations/36682332 | http://purl.uniprot.org/core/author | "Choi H.S."xsd:string |
| http://purl.uniprot.org/citations/36682332 | http://purl.uniprot.org/core/author | "Park S.S."xsd:string |
| http://purl.uniprot.org/citations/36682332 | http://purl.uniprot.org/core/author | "Park H.B."xsd:string |
| http://purl.uniprot.org/citations/36682332 | http://purl.uniprot.org/core/author | "Do H.A."xsd:string |
| http://purl.uniprot.org/citations/36682332 | http://purl.uniprot.org/core/date | "2023"xsd:gYear |
| http://purl.uniprot.org/citations/36682332 | http://purl.uniprot.org/core/name | "Biochem Biophys Res Commun"xsd:string |
| http://purl.uniprot.org/citations/36682332 | http://purl.uniprot.org/core/pages | "124-131"xsd:string |
| http://purl.uniprot.org/citations/36682332 | http://purl.uniprot.org/core/title | "Deubiquitinating enzyme YOD1 deubiquitinates and destabilizes alpha-synuclein."xsd:string |
| http://purl.uniprot.org/citations/36682332 | http://purl.uniprot.org/core/volume | "645"xsd:string |
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