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The Functions of Metamorphic Metallothioneins in Zinc and Copper Metabolism
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Int. J. Mol. Sci. 2017, 18(6), 1289; doi:10.3390/ijms18061289

Proteomic High Affinity Zn2+ Trafficking: Where Does Metallothionein Fit in?

Department of Chemistry and Biochemistry, University of Wisconsin–Milwaukee, Milwaukee, WI 53217, USA
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Received: 5 May 2017 / Revised: 7 June 2017 / Accepted: 9 June 2017 / Published: 17 June 2017
(This article belongs to the Special Issue Metallothioneins in Bioinorganic Chemistry: Recent Developments)
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Abstract

The cellular constitution of Zn-proteins and Zn-dependent signaling depend on the capacity of Zn2+ to find specific binding sites in the face of a plethora of other high affinity ligands. The most prominent of these is metallothionein (MT). It serves as a storage site for Zn2+ under various conditions, and has chemical properties that support a dynamic role for MT in zinc trafficking. Consistent with these characteristics, changing the availability of zinc for cells and tissues causes rapid alteration of zinc bound to MT. Nevertheless, zinc trafficking occurs in metallothionein-null animals and cells, hypothetically making use of proteomic binding sites to mediate the intracellular movements of zinc. Like metallothionein, the proteome contains a large concentration of proteins that strongly coordinate zinc. In this environment, free Zn2+ may be of little significance. Instead, this review sets forth the basis for the hypothesis that components of the proteome and MT jointly provide the platform for zinc trafficking. View Full-Text
Keywords: zinc; metallothionein; proteome; zinc trafficking; zinc protein; zinc signaling zinc; metallothionein; proteome; zinc trafficking; zinc protein; zinc signaling
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Petering, D.H.; Mahim, A. Proteomic High Affinity Zn2+ Trafficking: Where Does Metallothionein Fit in? Int. J. Mol. Sci. 2017, 18, 1289.

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