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http://purl.uniprot.org/citations/26152728http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26152728http://www.w3.org/2000/01/rdf-schema#comment"A mutation, L166P, in the cytosolic protein, PARK7/DJ-1, causes protein misfolding and is linked to Parkinson disease. Here, we identify the fission yeast protein Sdj1 as the orthologue of DJ-1 and calculate by in silico saturation mutagenesis the effects of point mutants on its structural stability. We also map the degradation pathways for Sdj1-L169P, the fission yeast orthologue of the disease-causing DJ-1 L166P protein. Sdj1-L169P forms inclusions, which are enriched for the Hsp104 disaggregase. Hsp104 and Hsp70-type chaperones are required for efficient degradation of Sdj1-L169P. This also depends on the ribosome-associated E3 ligase Ltn1 and its co-factor Rqc1. Although Hsp104 is absolutely required for proteasomal degradation of Sdj1-L169P aggregates, the degradation of already aggregated Sdj1-L169P occurs independently of Ltn1 and Rqc1. Thus, our data point to soluble Sdj1-L169P being targeted early by Ltn1 and Rqc1. The fraction of Sdj1-L169P that escapes this first inspection then forms aggregates that are subsequently cleared via an Hsp104- and proteasome-dependent pathway."xsd:string
http://purl.uniprot.org/citations/26152728http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m115.662312"xsd:string
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/author"Nielsen M.L."xsd:string
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/author"Kragelund B.B."xsd:string
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/author"Hartmann-Petersen R."xsd:string
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/author"Kriegenburg F."xsd:string
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/author"Lindorff-Larsen K."xsd:string
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/author"Papaleo E."xsd:string
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/author"Madsen C.T."xsd:string
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/author"Larsen I.B."xsd:string
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/author"Poulsen E.G."xsd:string
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/author"Mathiassen S.G."xsd:string
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/pages"21141-21153"xsd:string
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/title"A Two-step Protein Quality Control Pathway for a Misfolded DJ-1 Variant in Fission Yeast."xsd:string
http://purl.uniprot.org/citations/26152728http://purl.uniprot.org/core/volume"290"xsd:string
http://purl.uniprot.org/citations/26152728http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26152728
http://purl.uniprot.org/citations/26152728http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/26152728
http://purl.uniprot.org/uniprot/Q10356#attribution-EE7AFD77C0E2AEE55AD24A0F25BB72CEhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/26152728
http://purl.uniprot.org/uniprot/O74349#attribution-7A10A486B0FEDA0E1EDBD18749B3EA15http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/26152728
http://purl.uniprot.org/uniprot/O13796#attribution-7A10A486B0FEDA0E1EDBD18749B3EA15http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/26152728
http://purl.uniprot.org/uniprot/#_Q10356-mappedCitation-26152728http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26152728
http://purl.uniprot.org/uniprot/#_O74349-mappedCitation-26152728http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26152728