{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hoch E"],"funding":["NIGMS NIH HHS"],"pagination":["7202-7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3358884"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["109(19)"],"pubmed_abstract":["Zinc and cadmium are similar metal ions, but though Zn(2+) is an essential nutrient, Cd(2+) is a toxic and common pollutant linked to multiple disorders. Faster body turnover and ubiquitous distribution of Zn(2+) vs. Cd(2+) suggest that a mammalian metal transporter distinguishes between these metal ions. We show that the mammalian metal transporters, ZnTs, mediate cytosolic and vesicular Zn(2+) transport, but reject Cd(2+), thus constituting the first mammalian metal transporter with a refined selectivity against Cd(2+). Remarkably, the bacterial ZnT ortholog, YiiP, does not discriminate between Zn(2+) and Cd(2+). A phylogenetic comparison between the tetrahedral metal transport motif of YiiP and ZnTs identifies a histidine at the mammalian site that is critical for metal selectivity. Res"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Histidine pairing at the metal transport site of mammalian ZnT transporters controls Zn2+ over Cd2+ selectivity."],"pmcid":["PMC3358884"],"funding_grant_id":["R01 GM065137"],"pubmed_authors":["Fu D","Hoch E","Sekler I","Lin W","Chai J","Hershfinkel M"],"additional_accession":[]},"is_claimable":false,"name":"Histidine pairing at the metal transport site of mammalian ZnT transporters controls Zn2+ over Cd2+ selectivity.","description":"Zinc and cadmium are similar metal ions, but though Zn(2+) is an essential nutrient, Cd(2+) is a toxic and common pollutant linked to multiple disorders. Faster body turnover and ubiquitous distribution of Zn(2+) vs. Cd(2+) suggest that a mammalian metal transporter distinguishes between these metal ions. We show that the mammalian metal transporters, ZnTs, mediate cytosolic and vesicular Zn(2+) transport, but reject Cd(2+), thus constituting the first mammalian metal transporter with a refined selectivity against Cd(2+). Remarkably, the bacterial ZnT ortholog, YiiP, does not discriminate between Zn(2+) and Cd(2+). A phylogenetic comparison between the tetrahedral metal transport motif of YiiP and ZnTs identifies a histidine at the mammalian site that is critical for metal selectivity. Res","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 May","modification":"2025-04-04T14:32:12.577Z","creation":"2019-03-27T00:53:46Z"},"accession":"S-EPMC3358884","cross_references":{"pubmed":["22529353"],"doi":["10.1073/pnas.1200362109"]}}