Research Goal
Living systems host a crowd of molecular chaperones that act with different mechanisms and serve to maintain protein homeostasis. Our group studies nuclear and cytosolic chaperones. Among the cytosolic chaperones we are interested in members of the Hsp60, Hsp70 and Hsp100 families.
Publications
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Structural recognition and stabilization of tyrosine hydroxylase by the J-domain protein DNAJC12
Nat Commun. 2025 Mar 20;16(1):2755. doi: 10.1038/s41467-025-57733-6. PMID: 40113792; PMCID: PMC11926245. -
Pseudophosphorylation of single residues of the J-domain of DNAJA2 regulates the holding/folding balance of the Hsc70 system
Protein Sci. 2024 Aug;33(8):e5105. doi: 10.1002/pro.5105. PMID: 39012012; PMCID: PMC11249846. -
A Targetable N-Terminal Motif Orchestrates α-Synuclein Oligomer-to-Fibril Conversion
J Am Chem Soc. 2024 Apr 29. doi: 10.1021/jacs.4c02262. Epub ahead of print. PMID: 38683963. -
The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70
Nature Communications volume 14, Article number: 5436 (2023). DOI: 10.1038/s41467-023-41150-8 -
Quantitative super-resolution imaging of pathological aggregates reveals distinct toxicity profiles in different synucleinopathies
Proceedings of the National Academy of Sciences of the United States of America (2022) doi/10.1073/pnas.2205591119 -
Fine-tuning of the Hsc70-based human protein disaggregase machinery by the distinctive C-terminal extension of Apg2
Journal of Molecular Biology (2022), 167841, doi.org/10.1016/j.jmb.2022.167841 -
Truncation-Driven Lateral Association of α-Synuclein Hinders Amyloid Clearance by the Hsp70-based Disaggregase.
Int. J. Mol. Sci. 2021, 22(23), 12983; (2021) doi: 10.3390/ijms222312983 -
Unzipping the Secrets of Amyloid Disassembly by the Human Disaggregase
Cells. 2021 Oct 14;10(10):2745 DOI: 10.3390/cells10102745 -
All-or-none amyloid disassembly via chaperone-triggered fibril unzipping favors clearance of α-synuclein toxic species.
Proceedings of the National Academy of Sciences Sep 2021, 118 (36) e2105548118, (2021) doi: 10.1073/pnas.2105548118