Metallochaperones, an Intracellular Shuttle Service for Metal Ions
Open accessAbstract
Enzymes that employ transition metals as co-factors are housed in a wide variety of intracellular locations or are exported to the extracellular milieu. A key question then arises: how are specific metal co-factors transported to diverse locations and subsequently sorted into the correct metalloenzymes? The mechanisms by which these tasks are accomplished are just now being unraveled. A new family of soluble metal receptor proteins known as “metallochaperones ” is emerging that act in the intracellular trafficking of metal ions. Although transition elements can be quite toxic, these metal receptors are not detoxification proteins; they clearly function in a “chaperonelike” manner, guiding and protecting the metal ion while facilitating appropriate partnerships. Here we will review the most recent advances in our understanding of copper metallochaperones and discuss mechanisms that may be relevant to other
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This process provides a molecular basis for the function of copper storage proteins and metallochaperones in intracellular trafficking.
“This process provides a molecular basis for the function of copper storage proteins and metallochaperones in intracellular trafficking.218”
From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [218]
The Conclusions describe metallochaperones delivering copper safely to intracellular destinations, and the ATX1 section outlines a molecular mechanism for copper transfer. The Requirement for Copper Metallochaperones section describes metallothioneins as copper-chelating detoxification systems, but does not establish a trafficking function or molecular basis for copper storage proteins. The cited paper also cannot identify what the citing sentence means by “this process” without its antecedent. (LLM, conf=0.84)
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Research works printed but not linked: 6
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“oxidase and ceruloplasmin) acquire Cu in the Golgi before reaching their final destination [3,4,5].”
BackgroundInfluential
- Authors
- O'Halloran, T. V., & Culotta, V. C.
- Affiliations
- Johns Hopkins University (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-08
- Volume
- 275
- Issue
- 33
- Pages
- 25057-25060
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2103378158
- Cited by
- 806
- References
- 0
- Citations by year
- 2026: 12 · 2025: 15 · 2024: 17 · 2023: 18 · 2022: 23 · 2021: 17 · 2020: 18 · 2019: 21 · 2018: 33 · 2017: 25 · 2016: 29 · 2015: 23 · 2014: 29 · 2013: 26 · 2012: 36
- FWCI
- 7.06
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- ALS Association
- National Institutes of Health
- National Institute of General Medical Sciences (GM-54111, GM50016, R01GM054111, R01GM038784)
- National Institute of Environmental Health Sciences (R01ES008996, ES08996)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Heavy Metal Exposure and Toxicity
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- metallochaperone, copper chaperone, copper uptake, superoxide dismutase, SOD1, metalloenzymes, metal cofactors, copper toxicity, metal homeostasis, amyotrophic lateral sclerosis
- MeSH terms
- Animals, Biological Transport, Carrier Proteins, Copper, Fungal Proteins, Golgi Apparatus, Humans, Ions, Mitochondria, Models, Biological, Molecular Chaperones, Saccharomyces cerevisiae Proteins
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