Evidence map›Paper›PMID 32348750›Full record

ArticleCell reports2020

Molecular Basis of Zinc-Dependent Endocytosis of Human ZIP4 Transceptor.

Chi Zhang, Dexin Sui, Tuo Zhang, Jian Hu

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.6field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Metal Ion Signaling in Biomedicine.Chemical reviews · 2025
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Chi ZhangDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.
Dexin SuiDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.
Tuo ZhangDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.
Jian HuDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA; Department of Chemistry, Michigan State University, East Lansing, MI 48824, USA. Electronic address: hujian1@msu.edu.
Michigan State University · US

Funding

Zinc enrichment/zinc sensing mechanism through the extracellular domain of ZIP4R01GM115373 · NIGMS · MICHIGAN STATE UNIVERSITY · PI HU, JIAN · 2015 to 2019
$1.5M
Structural and Mechanistic Characterization of the ZIP Metal TransportersR01GM129004 · NIGMS · MICHIGAN STATE UNIVERSITY · PI HU, JIAN · 2018 to 2020
$593k
NIGMS NIH HHS R01 GM115373NIGMS NIH HHS R01 GM129004
6 · The paper itself

Abstract

Nutrient transporters can be rapidly removed from the cell surface via substrate-stimulated endocytosis as a way to control nutrient influx, but the molecular underpinnings are not well understood. In this work, we focus on zinc-dependent endocytosis of human ZIP4 (hZIP4), a zinc transporter that is essential for dietary zinc uptake. Structure-guided mutagenesis and internalization assay reveal that hZIP4 per se acts as the exclusive zinc sensor, with the transport site's being responsible for zinc sensing. In an effort of seeking sorting signal, a scan of the longest cytosolic loop (L2) leads to identification of a conserved Leu-Gln-Leu motif that is essential for endocytosis. Partial proteolysis of purified hZIP4 demonstrates a structural coupling between the transport site and the L2 upon zinc binding, which supports a working model of how zinc ions at physiological concentration trigger a conformation-dependent endocytosis of the zinc transporter. This work provides a paradigm on post-translational regulation of nutrient transporters.

Indexed as

Cation Transport ProteinsEndocytosisHEK293 CellsHumansZincCation Transport ProteinsSLC39A4 protein, humanZincendocytosisnutrient transportersorting signaltransceptorubiquitinationzinczinc transporterZIP4

Identifiers

PMID32348750
PMCPMC7661102
OpenAlexW3018834036

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.