The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Cytosolic zinc buffering and muffling: Their role in intracellular zinc homeostasis
Abstract
Our knowledge of the molecular mechanisms of intracellular homeostatic control of zinc ions is now firmly grounded on experimental findings gleaned from the study of zinc proteomes and metallomes, zinc transporters, and insights from the use of computational approaches. A cell's repertoire of zinc homeostatic molecules includes cytosolic zinc-binding proteins, transporters localized to cytoplasmic and organellar membranes, and sensors of cytoplasmic free zinc ions. Under steady state conditions, a primary function of cytosolic zinc-binding proteins is to buffer the relatively large zinc content found in most cells to a cytosolic zinc(ii) ion concentration in the picomolar range. Under non-steady state conditions, zinc-binding proteins and transporters act in concert to modulate transient changes in cytosolic zinc ion concentration in a process that is called zinc muffling. For example, if a cell is challenged by an influx of zinc ions, muffling reactions will dampen the resulting rise in cytosolic zinc ion concentration and eventually restore the cytosolic zinc ion concentration to its original value by shuttling zinc ions into subcellular stores or by removing zinc ions from the cell. In addition, muffling reactions provide a potential means to control changes in cytosolic zinc ion concentrations for purposes of cell signalling in what would otherwise be considered a buffered environment not conducive for signalling. Such intracellular zinc ion signals are known to derive from redox modifications of zinc-thiolate coordination environments, release from subcellular zinc stores, and zinc ion influx via channels. Recently, it has been discovered that metallothionein binds its seven zinc ions with different affinities. This property makes metallothionein particularly well positioned to participate in zinc buffering and muffling reactions. In addition, it is well established that metallothionein is a source of zinc ions under conditions of redox signalling. We suggest that the biological functions of transient changes in cytosolic zinc ion concentrations (presumptive zinc signals) complement those of calcium ions in both spatial and temporal dimensions.
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Cites
Femtomolar Sensitivity of Metalloregulatory Proteins Controlling Zinc Homeostasis
Outten, C. E., & O'Halloran, A. T. V. (2001) · Science · doi:10.1126/science.1060331 · Cited by 1,489
Metalloproteins and metal sensing
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Counting the Zinc-Proteins Encoded in the Human Genome
Andreini, C., Banci, L., Bertini, I., & Rosato, A. (2006) · Journal of Proteome Research · doi:10.1021/pr050361j · Cited by 1,109
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Zinc transporter ZIP8 (SLC39A8) and zinc influence IFN-γ expression in activated human T cells
Aydemir, T. B., Liuzzi, J. P., McClellan, S., & Cousins, R. J. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.1208759 · Cited by 229
Metallothionein in the central nervous system: Roles in protection, regeneration and cognition
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Cited by
Kambe, T., Tsuji, T., Hashimoto, A., & Itsumura, N. (2015) · Physiological Reviews · doi:10.1152/physrev.00035.2014 · Cited by 1,158
Small-Molecule Two-Photon Probes for Bioimaging Applications
Kim, H. M., & Cho, B. R. (2015) · Chemical Reviews · doi:10.1021/cr5004425 · Cited by 1,047
Zinc biochemistry: From a single zinc enzyme to a key element of life
Maret, W. (2013) · Advances in Nutrition · doi:10.3945/an.112.003038 · Cited by 818
Self-citationMetal homeostasis and resistance in bacteria
Chandrangsu, P., Rensing, C., & Helmann, J. D. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2017.15 · Cited by 812
The biological inorganic chemistry of zinc ions
Krężel, A., & Maret, W. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.04.010 · Cited by 768
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Metadata
- Authors
- Colvin, R. A., Holmes, W. R., Fontaine, C. P., & Maret, W.
- Venue
- Metallomics
- Publisher
- Oxford University Press (OUP)
- Published
- 2010
- Volume
- 2
- Issue
- 5
- Pages
- 306
- ISSN
- 1756-5901 (ISSN-L)
- 1756-591X
- OpenAlex
- W2043986265
- Cited by
- 428
- References
- 8
- FWCI
- 23.77
- Type
- journal article
- Language
- en
- Open access
- closed
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