Evidence map›Paper›PMID 32869741›Full record

ArticleeLife2020

Structural basis for the reaction cycle of DASS dicarboxylate transporters.

David B Sauer, Noah Trebesch, Jennifer J Marden, Nicolette Cocco, Jinmei Song, Akiko Koide, Shohei Koide, Emad Tajkhorshid, Da-Neng Wang

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

45 citing papers in PubMed, 73 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Elevator mechanism dynamics in a sodium-coupled dicarboxylate transporter.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Structural Mechanism of Prestin-Membrane Mechanotransduction.bioRxiv : the preprint server for biology · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Cryo-EM structures reveal the HLife science alliance · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

David B SauerSkirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, United States.ORCID 0000-0001-9291-4640
Noah TrebeschNIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, Department of Biochemistry, and Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, United States.ORCID 0000-0001-5536-4862
Jennifer J MardenSkirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, United States.
Nicolette CoccoSkirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, United States.
Jinmei SongSkirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, United States.
Akiko KoidePerlmutter Cancer Center, New York University School of Medicine, New York, United States.
Shohei KoidePerlmutter Cancer Center, New York University School of Medicine, New York, United States.
Emad TajkhorshidNIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, Department of Biochemistry, and Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, United States.ORCID 0000-0001-8434-1010
Da-Neng WangSkirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, United States.ORCID 0000-0002-6496-4699
New York University · USUniversity of Illinois Urbana-Champaign · US

Funding

WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2012 to 2021
$19.0M
Structural Genomics on Membrane ProteinsU54GM095315 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI ROST, BURKHARD · 2010 to 2014
$15.2M
Toolkit for High-Resolution Structure and Dynamics of Functional LipidsR01GM123455 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI MORRISSEY, JAMES H., RIENSTRA, CHAD M · 2016 to 2020
$5.0M
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
System-Level Simulation of a Bioenergetic MembraneR01GM067887 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2003 to 2018
$4.0M
Training program in Molecular BiophysicsT32GM088118 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI STOKES, DAVID L. · 2010 to 2019
$1.8M
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 P41 GM104601NIGMS NIH HHS R01 GM067887NIGMS NIH HHS R01 GM121994NIGMS NIH HHS R01 GM123455NIGMS NIH HHS T32 GM088118NIGMS NIH HHS U54 GM095315NINDS NIH HHS R01 NS108151
6 · The paper itself

Abstract

Citrate, α-ketoglutarate and succinate are TCA cycle intermediates that also play essential roles in metabolic signaling and cellular regulation. These di- and tricarboxylates are imported into the cell by the divalent anion sodium symporter (DASS) family of plasma membrane transporters, which contains both cotransporters and exchangers. While DASS proteins transport substrates via an elevator mechanism, to date structures are only available for a single DASS cotransporter protein in a substrate-bound, inward-facing state. We report multiple cryo-EM and X-ray structures in four different states, including three hitherto unseen states, along with molecular dynamics simulations, of both a cotransporter and an exchanger. Comparison of these outward- and inward-facing structures reveal how the transport domain translates and rotates within the framework of the scaffold domain through the transport cycle. Additionally, we propose that DASS transporters ensure substrate coupling by a charge-compensation mechanism, and by structural changes upon substrate release.

Indexed as

Cryoelectron MicroscopyCrystallography, X-RayDicarboxylic Acid TransportersEscherichia coliEscherichia coli ProteinsLactobacillus acidophilusMolecular Dynamics SimulationDicarboxylic Acid TransportersEscherichia coli Proteinscryo-EME. coliLactobacillus acidophilusmembrane protein structuremembrane transportmolecular biophysicsstructural biologyVibrio choleraeX-ray crystallography

Identifiers

PMID32869741
PMCPMC7553777
OpenAlexW3082443766

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.