Evidence map›Paper›PMID 30237557›Full record

ArticleScientific reports2018

Evaluation of the roles of the cytosolic N-terminus and His-rich loop of ZNT proteins using ZNT2 and ZNT3 chimeric mutants.

Kazuhisa Fukue, Naoya Itsumura, Natsuko Tsuji, Katsutoshi Nishino, Masaya Nagao, Hiroshi Narita, Taiho Kambe

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Loss of Znt8 function in diabetes mellitus: risk or benefit?Molecular and cellular biochemistry · 2021
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. A structural overview of the zinc transporters in the cation diffusion facilitator family.Acta crystallographica. Section D, Structural biology · 2019
    Review
  10. Article
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

7 authors at 2 institutions in 1 country.

Kazuhisa FukueDivision of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto, 606-8502, Japan.
Naoya ItsumuraDivision of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto, 606-8502, Japan.
Natsuko TsujiDivision of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto, 606-8502, Japan.
Katsutoshi NishinoDivision of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto, 606-8502, Japan.
Masaya NagaoDivision of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto, 606-8502, Japan.
Hiroshi NaritaDepartment of Food Science, Kyoto Women's University, Kyoto, 605-8501, Japan.
Taiho KambeDivision of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto, 606-8502, Japan. kambe1@kais.kyoto-u.ac.jp.ORCID 0000-0001-9757-063X
Kyoto University · JPKyoto Women's University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The physiological roles of Zn transporter (ZNT) proteins are being increasingly recognized, and three dimensional structures of ZNT bacterial homologs have facilitated our understanding of their biochemical characteristics at the molecular level. However, the biological role of the unique structural features of vertebrate ZNTs, which are absent in their bacterial homologues, is not completely understood. These ZNT sequences include a cytosolic His-rich loop between transmembrane helices IV and V and the cytosolic N-terminus. This study investigated the contribution of these features to zinc transport by ZNT proteins. The importance of the His residues in the cytosolic His-rich loop was investigated using ZNT2 Ala substitution and deletion mutants. The presence of His residues was not essential for zinc transport, even though they possibly participate in modulation of zinc transport activity. Furthermore, we determined the role of the N-terminus by characterizing ZNT2 and ZNT3 domain-swapped and deletion mutants. Unexpectedly, the N-terminus was also not essential for zinc transport by ZNT2 and the domain-swapped ZNT2 mutant, in which the cytosolic His-rich loop was substituted with that of ZNT3. These results provide molecular insights into understanding the roles of the cytosolic parts of ZNT2, ZNT3, and probably other members of their subgroup.

Indexed as

AnimalsCation Transport ProteinsCell LineChickensCytosolZincCation Transport ProteinsZinc

Identifiers

PMID30237557
PMCPMC6147782
OpenAlexW2891675306

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LicenceCC BY
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Registered trials

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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.