| http://purl.uniprot.org/citations/24063750 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24063750 | http://www.w3.org/2000/01/rdf-schema#comment | "The ubiquitin signaling pathway consists of hundreds of enzymes that are tightly regulated for the maintenance of cell homeostasis. Parkin is an E3 ubiquitin ligase responsible for conjugating ubiquitin onto a substrate protein, which itself can be ubiquitinated. Ataxin-3 performs the opposing function as a deubiquitinating enzyme that can remove ubiquitin from parkin. In this work, we have identified the mechanism of interaction between the ubiquitin-like (Ubl) domain from parkin and three C-terminal ubiquitin-interacting motifs (UIMs) in ataxin-3. (1)H-(15)N heteronuclear single-quantum coherence titration experiments revealed that there are weak direct interactions between all three individual UIM regions of ataxin-3 and the Ubl domain. Each UIM utilizes the exposed β-grasp surface of the Ubl domain centered around the I44 patch that did not vary in the residues involved or the surface size as a function of the number of ataxin-3 UIMs involved. Further, the apparent dissociation constant for ataxin-3 decreased as a function of the number of UIM regions used in experiments. A global multisite fit of the nuclear magnetic resonance titration data, based on three identical binding ligands, resulted in a KD of 669 ± 62 μM for each site. Our observations support a multivalent ligand binding mechanism employed by the parkin Ubl domain to recruit multiple UIM regions in ataxin-3 and provide insight into how these two proteins function together in ubiquitination-deubiquitination pathways."xsd:string |
| http://purl.uniprot.org/citations/24063750 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi400780v"xsd:string |
| http://purl.uniprot.org/citations/24063750 | http://purl.uniprot.org/core/author | "Shaw G.S."xsd:string |
| http://purl.uniprot.org/citations/24063750 | http://purl.uniprot.org/core/author | "Mercier P."xsd:string |
| http://purl.uniprot.org/citations/24063750 | http://purl.uniprot.org/core/author | "Barber K.R."xsd:string |
| http://purl.uniprot.org/citations/24063750 | http://purl.uniprot.org/core/author | "Safadi S.S."xsd:string |
| http://purl.uniprot.org/citations/24063750 | http://purl.uniprot.org/core/author | "Bai J.J."xsd:string |
| http://purl.uniprot.org/citations/24063750 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24063750 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/24063750 | http://purl.uniprot.org/core/pages | "7369-7376"xsd:string |
| http://purl.uniprot.org/citations/24063750 | http://purl.uniprot.org/core/title | "Ataxin-3 is a multivalent ligand for the parkin Ubl domain."xsd:string |
| http://purl.uniprot.org/citations/24063750 | http://purl.uniprot.org/core/volume | "52"xsd:string |
| http://purl.uniprot.org/citations/24063750 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24063750 |
| http://purl.uniprot.org/citations/24063750 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/24063750 |
| http://purl.uniprot.org/uniprot/P54252#attribution-6C27916AD1ECA76A1244FC2BE8A52776 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/24063750 |
| http://purl.uniprot.org/uniprot/O60260#attribution-6C27916AD1ECA76A1244FC2BE8A52776 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/24063750 |
| http://purl.uniprot.org/uniprot/#_O60260-mappedCitation-24063750 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24063750 |
| http://purl.uniprot.org/uniprot/O60260 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/24063750 |