ArticleThe Journal of biological chemistry2014
Interactions between metal-binding domains modulate intracellular targeting of Cu(I)-ATPase ATP7B, as revealed by nanobody binding.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- Effluxosomes and the evolution of metal resistance inInfection and immunity · 2026Review
- Tiny tools closing the gap: nanobodies in research and therapy.Function (Oxford, England) · 2026Review
- Multiscale computational genomics in Wilson disease: from atomic dynamics to clinical prediction.Frontiers in genetics · 2026Review
- Mammalian copper homeostasis: physiological roles and molecular mechanisms.Physiological reviews · 2025Review
- Functional Screen of Wilson Disease ATP7B Variants Reveals Residual Transport Activities.Human mutation · 2025Article
- The interplay between copper metabolism and microbes: in perspective of host copper-dependent ATPases ATP7A/B.Frontiers in cellular and infection microbiology · 2023Review
- Copper binding leads to increased dynamics in the regulatory N-terminal domain of full-length human copper transporter ATP7B.PLoS computational biology · 2022Article
- Mutation spectrum ofMolecular genetics and metabolism reports · 2022Article
- Easily Established and Multifunctional Synthetic Nanobody Libraries as Research Tools.International journal of molecular sciences · 2022Review
- At sixes and sevens: cryptic domain in the metal binding chain of the human copper transporter ATP7A.Biophysical journal · 2021Article
- A guide to: generation and design of nanobodies.The FEBS journal · 2021Review
- Nanobodies against the metal binding domains of ATP7B as tools to study copper transport in the cell.Metallomics : integrated biometal science · 2020Article
- Analysis of Wilson disease mutations revealed that interactions between different ATP7B mutants modify their properties.Scientific reports · 2020Article
- An EPR Study on the Interaction between the Cu(I) Metal Binding Domains of ATP7B and the Atox1 Metallochaperone.International journal of molecular sciences · 2020Article
- Human glutaredoxin-1 can transfer copper to isolated metal binding domains of the PScientific reports · 2020Article
- Nanobody-Based Probes for Subcellular Protein Identification and Visualization.Frontiers in cellular neuroscience · 2020Review
- The Structure of Metal Binding Domain 1 of the Copper Transporter ATP7B Reveals Mechanism of a Singular Wilson Disease Mutation.Scientific reports · 2018Article
- 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 metal chaperone Atox1 regulates the activity of the human copper transporter ATP7B by modulating domain dynamics.The Journal of biological chemistry · 2017Article
- Disease-causing point-mutations in metal-binding domains of Wilson disease protein decrease stability and increase structural dynamics.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2017Article
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 3 countries.
Funding
Abstract
The biologically and clinically important membrane transporters are challenging proteins to study because of their low level of expression, multidomain structure, and complex molecular dynamics that underlies their activity. ATP7B is a copper transporter that traffics between the intracellular compartments in response to copper elevation. The N-terminal domain of ATP7B (N-ATP7B) is involved in binding copper, but the role of this domain in trafficking is controversial. To clarify the role of N-ATP7B, we generated nanobodies that interact with ATP7B in vitro and in cells. In solution NMR studies, nanobodies revealed the spatial organization of N-ATP7B by detecting transient functionally relevant interactions between metal-binding domains 1-3. Modulation of these interactions by nanobodies in cells enhanced relocalization of the endogenous ATP7B toward the plasma membrane linking molecular and cellular dynamics of the transporter. Stimulation of ATP7B trafficking by nanobodies in the absence of elevated copper provides direct evidence for the important role of N-ATP7B structural dynamics in regulation of ATP7B localization in a cell.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.