ArticleThe Journal of biological chemistry2015
A Two-step Protein Quality Control Pathway for a Misfolded DJ-1 Variant in Fission Yeast.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Synonymous mutations in the phosphoglycerate kinase 1 gene induce an altered response to protein misfolding inFrontiers in microbiology · 2022Article
- Folliculin variants linked to Birt-Hogg-Dubé syndrome are targeted for proteasomal degradation.PLoS genetics · 2020Article
- Article
- Computational Structural Biology ofFrontiers in oncology · 2018Review
- Amyotrophic lateral sclerosis as a protein level, non-genomic disease: Therapy with S2RM exosome released molecules.World journal of stem cells · 2017Review
- A non-transcriptional role for the glucocorticoid receptor in mediating the cell stress response.Scientific reports · 2017Article
- The exocyst subunit Sec3 is regulated by a protein quality control pathway.The Journal of biological chemistry · 2017Article
- Predicting the impact of Lynch syndrome-causing missense mutations from structural calculations.PLoS genetics · 2017Article
- UBL/BAG-domain co-chaperones cause cellular stress upon overexpression through constitutive activation of Hsf1.Cell stress & chaperones · 2017Article
- The Mutational Landscape of the Oncogenic MZF1 SCAN Domain in Cancer.Frontiers in molecular biosciences · 2016Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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