2. Academic Validation
  3. Structure-function analysis of a novel member of the LIV-1 subfamily of zinc transporters, ZIP14

Structure-function analysis of a novel member of the LIV-1 subfamily of zinc transporters, ZIP14

  • FEBS Lett. 2005 Jan 17;579(2):427-32. doi: 10.1016/j.febslet.2004.12.006.
K M Taylor 1,  H E Morgan,  A Johnson,  R I Nicholson
Affiliations

Affiliation

  • 1 Tenovus Cancer Research Centre, Welsh School of Pharmacy, Cardiff University, Redwood Building, King Edward VII avenue, Cardiff CF10 3XF, UK. Taylorkm@cardiff.ac.uk
PMID: 15642354 DOI: 10.1016/j.febslet.2004.12.006
Abstract

Here, we report the first investigation of a novel member of the LZT (LIV-1 subfamily of ZIP zinc Transporters) subfamily of zinc influx transporters. LZT subfamily sequences all contain a unique and highly conserved metalloprotease motif (HEXPHEXGD) in transmembrane domain V with both histidine residues essential for zinc transport by ZIP (Zrt-, Irt-like Proteins) transporters. We investigate here whether ZIP14 (SLC39A14), lacking the initial histidine in this motif, is still able to transport zinc. We demonstrate that this plasma membrane located glycosylated protein functions as a zinc influx transporter in a temperature-dependant manner.

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