Evidence map›Paper›PMID 38956111›Full record

ArticleNature communications2024

Dimeric transport mechanism of human vitamin C transporter SVCT1.

Takaaki A Kobayashi, Hiroto Shimada, Fumiya K Sano, Yuzuru Itoh, Sawako Enoki, Yasushi Okada, Tsukasa Kusakizako, Osamu Nureki

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Article
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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

8 authors.

Takaaki A KobayashiDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.ORCID 0009-0007-4740-006X
Hiroto ShimadaDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Fumiya K SanoDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-8965-788X
Yuzuru ItohDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.ORCID 0000-0001-7802-5572
Sawako EnokiDepartment of Physics, and Universal Biology Institute (UBI), Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Yasushi OkadaDepartment of Physics, and Universal Biology Institute (UBI), Graduate School of Science, The University of Tokyo, Tokyo, Japan.ORCID 0000-0003-2601-3689
Tsukasa KusakizakoDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan. kusakizako@bs.s.u-tokyo.ac.jp.ORCID 0000-0002-6186-6647
Osamu NurekiDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan. nureki@bs.s.u-tokyo.ac.jp.ORCID 0000-0003-1813-7008

Funding

Japan Agency for Medical Research and Development (AMED) JP23ama121002MEXT | Japan Science and Technology Agency (JST) 20344981
6 · The paper itself

Abstract

Vitamin C plays important roles as a cofactor in many enzymatic reactions and as an antioxidant against oxidative stress. As some mammals including humans cannot synthesize vitamin C de novo from glucose, its uptake from dietary sources is essential, and is mediated by the sodium-dependent vitamin C transporter 1 (SVCT1). Despite its physiological significance in maintaining vitamin C homeostasis, the structural basis of the substrate transport mechanism remained unclear. Here, we report the cryo-EM structures of human SVCT1 in different states at 2.5-3.5 Å resolutions. The binding manner of vitamin C together with two sodium ions reveals the counter ion-dependent substrate recognition mechanism. Furthermore, comparisons of the inward-open and occluded structures support a transport mechanism combining elevator and distinct rotational motions. Our results demonstrate the molecular mechanism of vitamin C transport with its underlying conformational cycle, potentially leading to future industrial and medical applications.

Indexed as

Ascorbic AcidCryoelectron MicroscopySodium-Coupled Vitamin C TransportersBiological TransportHEK293 CellsHumansModels, MolecularProtein BindingProtein ConformationProtein MultimerizationSodiumAscorbic AcidSLC23A1 protein, humanSodiumSodium-Coupled Vitamin C Transporters

Identifiers

PMID38956111
PMCPMC11219872

What OpenQuestion holds

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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.