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The Functions of Metallothionein and ZIP and ZnT Transporters: An Overview and Perspective

Open access
Kimura, Tomoki, Kambe, Taiho·2016·International Journal of Molecular Sciences

Abstract

Around 3000 proteins are thought to bind zinc in vivo, which corresponds to ~10% of the human proteome. Zinc plays a pivotal role as a structural, catalytic, and signaling component that functions in numerous physiological processes. It is more widely used as a structural element in proteins than any other transition metal ion, is a catalytic component of many enzymes, and acts as a cellular signaling mediator. Thus, it is expected that zinc metabolism and homeostasis have sophisticated regulation, and elucidating the underlying molecular basis of this is essential to understanding zinc functions in cellular physiology and pathogenesis. In recent decades, an increasing amount of evidence has uncovered critical roles of a number of proteins in zinc metabolism and homeostasis through influxing, chelating, sequestrating, coordinating, releasing, and effluxing zinc. Metallothioneins (MT) and Zrt- and Irt-like proteins (ZIP) and Zn transporters (ZnT) are the proteins primarily involved in these processes, and their malfunction has been implicated in a number of inherited diseases such as acrodermatitis enteropathica. The present review updates our current understanding of the biological functions of MTs and ZIP and ZnT transporters from several new perspectives.

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Metadata

Authors
Kimura, T., & Kambe, T.
Venue
International Journal of Molecular Sciences
Publisher
MDPI AG
Published
2016-03-04
Volume
17
Issue
3
Pages
336
ISSN
1422-0067 (ISSN-L)
OpenAlex
W2288699132
Cited by
409
References
14
FWCI
33.92
Type
journal article
Language
en
Open access
gold

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