Evidence map›Paper›PMID 34403567›Full record

ArticleThe FEBS journal2022

The ups and downs of elevator-type di-/tricarboxylate membrane transporters.

David B Sauer, Bing Wang, Joseph C Sudar, Jinmei Song, Jennifer Marden, William J Rice, Da-Neng Wang

Open access · bronzeAbstract read
In one paragraph

Article in The FEBS journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
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  6. Elevator mechanism dynamics in a sodium-coupled dicarboxylate transporter.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  12. 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

7 authors at 3 institutions in 2 countries.

David B SauerSkirball Institute of Biomolecular Medicine, New York University School of Medicine, NY, USA.
Bing WangCryo-Electron Microscopy Core, New York University School of Medicine, NY, USA.
Joseph C SudarSkirball Institute of Biomolecular Medicine, New York University School of Medicine, NY, USA.
Jinmei SongSkirball Institute of Biomolecular Medicine, New York University School of Medicine, NY, USA.
Jennifer MardenSkirball Institute of Biomolecular Medicine, New York University School of Medicine, NY, USA.
William J RiceCryo-Electron Microscopy Core, New York University School of Medicine, NY, USA.
Da-Neng WangSkirball Institute of Biomolecular Medicine, New York University School of Medicine, NY, USA.ORCID 0000-0002-6496-4699
New York University · USNew York Structural Biology Center · USUniversity of Oxford · GB

Funding

Transport Cycle and Inhibition of Human Na+-dicarboxylate Cotransporter NaDC3R01NS108151 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DANENG WANG · 2018 to 2026
$4.1M
Structural basis of the Ragulator-Rag GTPase complex as a platform for mTOR activation on the lysosomal surfaceR01GM121994 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DANENG · 2017 to 2020
$1.5M
Structural and mechanistic studies of INDY proteinsR01DK099023 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DANENG · 2013 to 2016
$1.5M
NIDDK NIH HHS R01 DK099023NIGMS NIH HHS R01 GM121994NINDS NIH HHS R01 NS108151
6 · The paper itself

Abstract

The divalent anion sodium symporter (DASS) family contains both sodium-driven anion cotransporters and anion/anion exchangers. The family belongs to a broader ion transporter superfamily (ITS), which comprises 24 families of transporters, including those of AbgT antibiotic efflux transporters. The human proteins in the DASS family play major physiological roles and are drug targets. We recently determined multiple structures of the human sodium-dependent citrate transporter (NaCT) and the succinate/dicarboxylate transporter from Lactobacillus acidophilus (LaINDY). Structures of both proteins show high degrees of structural similarity to the previously determined VcINDY fold. Conservation between these DASS protein structures and those from the AbgT family indicates that the VcINDY fold represents the overall protein structure for the entire ITS. The new structures of NaCT and LaINDY are captured in the inward- or outward-facing conformations, respectively. The domain arrangements in these structures agree with a rigid body elevator-type transport mechanism for substrate translocation across the membrane. Two separate NaCT structures in complex with a substrate or an inhibitor allowed us to explain the inhibition mechanism and propose a detailed classification scheme for grouping disease-causing mutations in the human protein. Structural understanding of multiple kinetic states of DASS proteins is a first step toward the detailed characterization of their entire transport cycle.

Indexed as

Membrane Transport ProteinsSymportersAnionsDicarboxylic Acid TransportersHumansSodiumAnionsDicarboxylic Acid TransportersMembrane Transport ProteinsSodiumSymporterscitrate uptakeDASS familyITSmembrane transporter structureSLC13 family

Identifiers

PMID34403567
PMCPMC9832446
OpenAlexW3196159109

What OpenQuestion holds

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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.