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The zinc transporter SLC39A7 (ZIP7) harbours a highly-conserved histidinerich N-terminal region that potentially contributes to zinc homeostasis in the endoplasmic reticulum

Adulcikas, J ORCID: 0000-0001-9193-6709, Norouzi, S ORCID: 0000-0002-7504-8581, Bretag, L, Sohal, SS ORCID: 0000-0001-9627-6498 and Myers, S ORCID: 0000-0003-4793-3820 2018 , 'The zinc transporter SLC39A7 (ZIP7) harbours a highly-conserved histidinerich N-terminal region that potentially contributes to zinc homeostasis in the endoplasmic reticulum' , Computers in Biology and Medicine, vol. 100 , pp. 196-202 , doi: 10.1016/j.compbiomed.2018.07.007.

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Abstract

The zinc transporter SLC39A7 (ZIP7)1 is a resident endoplasmic reticulum (ER) protein that is involved incontrolling the release of zinc from this organelle into the cytosol. Subsequently, zinc plays a major role inprocesses that preserve cellular homeostasis. The ER contains a high concentration of zinc, and under normalphysiological responses, maintains ER function. Disturbances in the concentration and distribution of zinc in theER leads to abnormal processes that typify many disease states. ZIP7 is protective against ER stress and is acritical ‘gate-keeper’ of zinc release from the ER during processes that require cellular maintenance. However, itis not known how ZIP7 achieves this protective activity while maintaining cellular function. Bioinformaticsanalysis was utilised to determine the relationship between ZIP7 and other zinc transporters across humans andthe animal and plant kingdom to determine the structure of this transporter in binding zinc in the ER. Analysis ofthe amino acid sequence of ZIP7 revealed several potential histidine binding sites for zinc in the N-terminalregion that were significantly different in comparison to the other members of this family. Moreover, this histidine-richregion in the N-terminal of ZIP7 was highly conserved across the animal and plant kingdom. Accordingly,the highly conserved histidine-rich region in the N-termini of ZIP7 across the animal and plantkingdom suggests that this domain has critical function(s). We hypothesise that ER-localized ZIP7 can potentiallysequester zinc to these histidine-rich regions and therefore provides a mechanism that is protective of thiscellular structure.

Item Type: Article
Authors/Creators:Adulcikas, J and Norouzi, S and Bretag, L and Sohal, SS and Myers, S
Keywords: zinc, endoplasmic reticulum stress, bioinformatics
Journal or Publication Title: Computers in Biology and Medicine
Publisher: Pergamon-Elsevier Science Ltd
ISSN: 0010-4825
DOI / ID Number: 10.1016/j.compbiomed.2018.07.007
Copyright Information:

Copyright 2018 Published by Elsevier Ltd.

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