Metallochaperones, an Intracellular Shuttle Service for Metal Ions*

By T. O’Halloran, V. Culotta. Journal of Biological Chemistry, 2000

768 citations recorded by the source corpus.

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 essential, yet potentially toxic, metal ions.

Subfields: Neurology, Nutrition and Dietetics, Physiology

View Paper: https://www.semanticscholar.org/paper/a7f95f8d3d08e5750ac62f8411f2f955b477fcb7

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In Neurology

1. S. Clemens
2. Ute Krämer
3. I. Yruela

In Nutrition and Dietetics

1. S. Clemens
2. G. Grass
3. C. Rensing
4. Ute Krämer
5. I. Yruela
6. J. Lloyd

In Physiology

1. S. Clemens
2. I. Yruela

Citations in the corpus

• Copper in plants: acquisition, transport and interactions. (2009, background): “…of cytosolic, soluble, low-molecular-weight metalreceptors proteins named metallochaperones that are involved in the intracellular trafficking of metal ions and insert the Cu into the active sites of specific partners, Cu-dependent enzymes (O´Halloran and Culotta 2000; Huffman and O`Halloran 2001).”
• Superoxide Dismutases: Role in Redox Signaling, Vascular Function, and Diseases (2011, neutral): “It consists of three functionally distinct protein domains (I, II, III) (172, 202) (Fig.”
• Physiological functions of mineral micronutrients (Cu, Zn, Mn, Fe, Ni, Mo, B, Cl). (2009, background): “However, part of the imported copper bypasses this system and becomes captured by small binding proteins, so called copper chaperones [2 ,12] that spare copper from the detoxification systems and guide it to the target sites in the cell.”
• Bacterial mercury resistance from atoms to ecosystems. (2003, background): “Similar primary and secondary structural components are also found in small intracellular proteins, the so-called metal chaperones, which function in the insertion of metal cofactors in redox-active enzymes in eukaryotes [166].”
• Heavy Metals and Human Health: Mechanistic Insight into Toxicity and Counter Defense System of Antioxidants (2015, background): “As such, its uptake, followed by distribution and utilization, and finally excretion from the body needs to be tightly regulated [234,235].”
• Physiology and molecular biology of stress tolerance in plants (2006, background): “…has evolved over time that functions in maintaining concentrations of essential metal ions in different cellular compartments within a narrow physiological range, thus minimizing the damage caused by entry of non-essential metal ions into the cytosol (Halloran and Cullota, 2000; Clemens, 2001).”
• Metal hyperaccumulation and bioremediation (2007, background): “With the recent identification of Cu chaperones and Cu transporters from S. cerevisiae and human, intracellular metal trafficking pathways are emerging (reviewed by O’Halloran and Cullota 2000).”
• Escherichia coli mechanisms of copper homeostasis in a changing environment. (2003, background): “Iron oxidation prior to uptake was experimentally determined to be the function of Fet3, a multi-copper oxidase from yeast S. cerevisiae [98].”
• Functions and Homeostasis of Zinc, Copper, and Nickel in plants (2005, background): “Instead, specific distribution systems ensure delivery of Cu ions to Curequiring organelles and proteins (O'Halloran and Culotta 2000).”