Evidence map›Paper›PMID 42085731›Full record

ArticleJournal of inorganic biochemistry2026

Cu(I) and Cu(II) binding by hyperactive variants of the human CTR1 N-terminus: Insights from cellular and model peptide studies.

Kaylee Ruth, Emily Post, Xiaobin Wu, Heejeong Kim, M Jake Pushie, Maria Escobedo, Kristin Kuter, Jaekwon Lee, Kathryn L Haas

Abstract read
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In one paragraph

Article in Journal of inorganic biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

9 authors.

Kaylee RuthDepartment of Chemistry, Duke University, Durham, NC 27708, USA.
Emily PostDepartment of Chemistry, Duke University, Durham, NC 27708, USA.
Xiaobin WuRedox Biology Center, Department of Biochemistry, University of Nebraska, Lincoln, NE 68588-0664, USA; Development Center of Plant Germplasm Resources, College of Life Sciences, Shanghai Normal University, Shanghai 200234, China.
Heejeong KimRedox Biology Center, Department of Biochemistry, University of Nebraska, Lincoln, NE 68588-0664, USA.
M Jake PushieDepartment of Surgery, University of Saskatchewan, Saskatoon, SK S7N 5E5, Canada.
Maria EscobedoDepartment of Mathematics and Computer Science, Saint Mary's College, Notre Dame, IN 46556, USA.
Kristin KuterDepartment of Mathematics and Computer Science, Saint Mary's College, Notre Dame, IN 46556, USA.
Jaekwon LeeRedox Biology Center, Department of Biochemistry, University of Nebraska, Lincoln, NE 68588-0664, USA.
Kathryn L HaasDepartment of Chemistry, Duke University, Durham, NC 27708, USA. Electronic address: kathryn.haas@duke.edu.

Funding

Mechanistic insights into homeostatic copper acquistionR01DK079209 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI LEE, JAEKWON · 2007 to 2014
$1.9M
NIDDK NIH HHS R01 DK079209
6 · The paper itself

Abstract

Copper (Cu) trafficking requires precise control of Cu(II)/Cu(I) redox chemistry to enable cellular acquisition while preventing toxicity. Human Cu transporter 1 protein (hCTR1) mediates cellular Cu uptake, yet key molecular details governing its extracellular Cu acquisition remain unresolved. Although hCTR1 is a Cu(I)-selective pore, extracellular Cu may be presented by carriers in the Cu(II) oxidation state. The N-terminal ectodomain of hCTR1 contains adjacent high-affinity Cu(II) and Cu(I)-binding sites that are proposed to facilitate Cu(II) reduction prior to transport. To investigate the role of residues in mediating Cu uptake, we combined cellular screening for hCtr1 mutations that confer enhanced Cu uptake phenotypes with spectroscopic studies of model peptides. We identified four site-specific substitutions within the distal ectodomain (D2N, M7T, G8E, and M9T) that increase cellular Cu uptake. Using model peptides corresponding to the first 14 residues of hCTR1 (hCTR

Indexed as

Cation Transport ProteinsCopperPeptidesBinding SitesCopper Transporter 1HumansMutationProtein BindingCation Transport ProteinsCopperCopper Transporter 1PeptidesSLC31A1 protein, humanCellular copper uptakeHuman CTR1Metal traffickingModel peptidesX-ray absorption spectroscopyYeast cellular screening

Identifiers

PMID42085731
PMCPMC13292886

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.