ArticleThe journal of physical chemistry. B2019
Biophysical Consequences of EVEN-PLUS Syndrome Mutations for the Function of Mortalin.
Article in The journal of physical chemistry. B, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 10 citations in OpenAlex.
- Tryptoline stereoprobe elaboration identifies inhibitors of the GRPEL1-HSPA9 complex.Nature chemical biology · 2026Article
- A post-translational regulatory map of chronic antigen-driven human T cell dysfunction.bioRxiv : the preprint server for biology · 2026Article
- Tryptoline Stereoprobe Elaboration Identifies Inhibitors of the GRPEL1-HSPA9 Chaperone Complex.bioRxiv : the preprint server for biology · 2025Article
- Structural insights into GrpEL1-mediated nucleotide and substrate release of human mitochondrial Hsp70.Nature communications · 2024Article
- Structural insights into GrpEL1-mediated nucleotide and substrate release of human mitochondrial Hsp70.bioRxiv : the preprint server for biology · 2024Article
- A new phenotype of EVEN-PLUS syndrome in a Chinese family and literature review.Molecular genetics & genomic medicine · 2024Review
- Identifying patients with EVEN-plus syndrome using exome sequencing and clinical feature analysis: A case report.Molecular genetics & genomic medicine · 2022Article
- Neutron crystallographic analysis of the nucleotide-binding domain of Hsp72 in complex with ADP.IUCrJ · 2022Article
- Improved Interpretation of Protein Conformational Differences and Ligand Occupancy in Large-Scale Cross-Link Data.Journal of proteome research · 2022Article
- Skeletal Phenotypes Due to Abnormalities in Mitochondrial Protein Homeostasis and Import.International journal of molecular sciences · 2020Review
- 2- and N6-functionalized adenosine-5'-diphosphate analogs for the inhibition of mortalin.FEBS letters · 2019Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
HSPA9, the gene coding for the mitochondrial chaperone mortalin, is involved in various cellular roles such as mitochondrial protein import, folding, degradation, Fe-S cluster biogenesis, mitochondrial homeostasis, and regulation of the antiapoptotic protein p53. Mutations in the HSPA9 gene, particularly within the region coding for the nucleotide-binding domain (NBD), cause the autosomal disorder known as EVEN-PLUS syndrome. The resulting mutants R126W and Y128C are located on the surface of the mortalin-NBD near the binding interface with the interdomain linker (IDL). We used differential scanning fluorimetry (DSF), biolayer interferometry, X-ray crystallography, ATP hydrolysis assays, and Rosetta docking simulations to study the structural and functional consequences of the EVEN-PLUS syndrome-associated R126W and Y128C mutations within the mortalin-NBD. These results indicate that the surface mutations R126W and Y128C have far-reaching effects that disrupt ATP hydrolysis, interdomain linker binding, and thermostability and increase the propensity for aggregation. The structural differences observed provide insight into how the conformations of mortalin differ from other heat shock protein 70 (Hsp70) homologues. Combined, our biophysical and structural studies contribute to the understanding of the molecular basis for how disease-associated mortalin mutations affect mortalin functionality and the pathogenesis of EVEN-PLUS syndrome.
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Registered trials
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