caa a22 4500 445321539 CHVBK 20180317142705.0 cr unu---uuuuu 170323e20110601xx s 000 0 eng 10.1007/s10534-010-9406-1 doi (NATIONALLICENCE)springer-10.1007/s10534-010-9406-1 Maret Wolfgang King's College London, Diabetes and Nutritional Sciences Division, 150 Stamford Street, SE1 9NH, London, UK aut Metals on the move: zinc ions in cellular regulation and in the coordination dynamics of zinc proteins [Elektronische Daten] [Wolfgang Maret] Homeostatic control maintains essential transition metal ions at characteristic cellular concentrations to support their physiological functions and to avoid adverse effects. Zinc is especially widely used as a catalytic or structural cofactor in about 3000 human zinc proteins. In addition, the homeostatic control of zinc in eukaryotic cells permits functions of zinc(II) ions in regulation and in paracrine and intracrine signaling. Zinc ions are released from proteins through ligand-centered reactions in zinc/thiolate coordination environments, and from stores in cellular organelles, where zinc transporters participate in zinc loading and release. Muffling reactions allow zinc ions to serve as signaling ions (second messengers) in the cytosol that is buffered to picomolar zinc ion concentrations at steady-state. Muffling includes zinc ion binding to metallothioneins, cellular translocations of metallothioneins, delivery of zinc ions to transporter proteins, and zinc ion fluxes through cellular membranes with the result of removing the additional zinc ions from the cytosol and restoring the steady-state. Targets of regulatory zinc ions are proteins with sites for transient zinc binding, such as membrane receptors, enzymes, protein-protein interactions, and sensor proteins that control gene expression. The generation, transmission, targets, and termination of zinc ion signals involve proteins that use coordination dynamics in the inner and outer ligand spheres to control metal ion association and dissociation. These new findings establish critically important functions of zinc ions and zinc metalloproteins in cellular control. Springer Science+Business Media, LLC., 2011 Zinc nationallicence Signaling nationallicence Metallothionein nationallicence Muffling nationallicence Buffering nationallicence ER : Endoplasmic reticulum nationallicence ERK : Extracellular signal-regulated kinase nationallicence IP3 : Inositol 1,4,5-trisphosphate nationallicence MT : Metallothionein nationallicence MTF-1 : Metal-response element (MRE)-binding transcription factor-1 nationallicence ZnT : Zinc transporter nationallicence BioMetals Springer Netherlands 24/3(2011-06-01), 411-418 0966-0844 24:3<411 2011 24 10534 https://doi.org/10.1007/s10534-010-9406-1 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10534-010-9406-1 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Maret Wolfgang King's College London, Diabetes and Nutritional Sciences Division, 150 Stamford Street, SE1 9NH, London, UK aut NATIONALLICENCE 773 0- BioMetals Springer Netherlands 24/3(2011-06-01), 411-418 0966-0844 24:3<411 2011 24 10534 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer