ArticleJournal of the American Chemical Society2012
Dynamic multibody protein interactions suggest versatile pathways for copper trafficking.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Human CTR1 Through the Ages: Milestones and Emerging Roles in Disease and Therapy.Biomolecules · 2025Review
- Molecular mechanism and structural models of protein-mediated copper transfer to the Arabidopsis thaliana ethylene receptor ETR1 at the ER membrane.Scientific reports · 2025Article
- A primer on copper biology in the brain.Neurobiology of disease · 2025Review
- A 'through-DNA' mechanism for co-regulation of metal uptake and efflux.Nature communications · 2024Article
- Structure and dimerization properties of the plant-specific copper chaperone CCH.Scientific reports · 2024Article
- Breakdown of Langmuir Adsorption Isotherm in Small Closed Systems.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- Chromatographic detection of low-molecular-mass metal complexes in the cytosol of Saccharomyces cerevisiae.Metallomics : integrated biometal science · 2020Article
- Copper trafficking in eukaryotic systems: current knowledge from experimental and computational efforts.Current opinion in structural biology · 2019Review
- Unraveling the Impact of Cysteine-to-Serine Mutations on the Structural and Functional Properties of Cu(I)-Binding Proteins.International journal of molecular sciences · 2019Article
- Ratiometric two-photon microscopy reveals attomolar copper buffering in normal and Menkes mutant cells.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Trapping intermediates in metal transfer reactions of the CusCBAF export pump ofCommunications biology · 2018Article
- Glutathione limits aquacopper(I) to sub-femtomolar concentrations through cooperative assembly of a tetranuclear cluster.The Journal of biological chemistry · 2017Article
- The six metal binding domains in human copper transporter, ATP7B: molecular biophysics and disease-causing mutations.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2017Review
- The structural flexibility of the human copper chaperone Atox1: Insights from combined pulsed EPR studies and computations.Protein science : a publication of the Protein Society · 2017Article
- Single-molecule dynamics and mechanisms of metalloregulators and metallochaperones.Biochemistry · 2013Review
- Crosstalk between Cu(I) and Zn(II) homeostasis via Atx1 and cognate domains.Chemical communications (Cambridge, England) · 2013Article
- Probing the coordination environment of the human copper chaperone HAH1: characterization of Hg(II)-bridged homodimeric species in solution.Chemistry (Weinheim an der Bergstrasse, Germany) · 2013Article
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8 authors.
Funding
Abstract
As part of intracellular copper trafficking pathways, the human copper chaperone Hah1 delivers Cu(+) to the Wilson's Disease Protein (WDP) via weak and dynamic protein-protein interactions. WDP contains six homologous metal binding domains (MBDs) connected by flexible linkers, and these MBDs all can receive Cu(+) from Hah1. The functional roles of the MBD multiplicity in Cu(+) trafficking are not well understood. Building on our previous study of the dynamic interactions between Hah1 and the isolated fourth MBD of WDP, here we study how Hah1 interacts with MBD34, a double-domain WDP construct, using single-molecule fluorescence resonance energy transfer (smFRET) combined with vesicle trapping. By alternating the positions of the smFRET donor and acceptor, we systematically probed Hah1-MBD3, Hah1-MBD4, and MBD3-MBD4 interaction dynamics within the multidomain system. We found that the two interconverting interaction geometries were conserved in both intermolecular Hah1-MBD and intramolecular MBD-MBD interactions. The Hah1-MBD interactions within MBD34 are stabilized by an order of magnitude relative to the isolated single-MBDs, and thermodynamic and kinetic evidence suggest that Hah1 can interact with both MBDs simultaneously. The enhanced interaction stability of Hah1 with the multi-MBD system, the dynamic intramolecular MBD-MBD interactions, and the ability of Hah1 to interact with multiple MBDs simultaneously suggest an efficient and versatile mechanism for the Hah1-to-WDP pathway to transport Cu(+).
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