Evidence map›Paper›PMID 31282475›Full record

ArticleActa crystallographica. Section D, Structural biology2019

LAT1 (SLC7A5) and CD98hc (SLC3A2) complex dynamics revealed by single-particle cryo-EM.

George N Chiduza, Rachel M Johnson, Gareth S A Wright, Svetlana V Antonyuk, Stephen P Muench, S Samar Hasnain

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 23 citations in OpenAlex.

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  12. Methods and protocols · 2021
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  13. Principal component analysis is limited to low-resolution analysis in cryoEM.Acta crystallographica. Section D, Structural biology · 2021
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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

6 authors at 2 institutions in 1 country.

George N ChiduzaMolecular Biophysics Group, Institute of Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 7ZB, England.
Rachel M JohnsonSchool of Biomedical Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, England.
Gareth S A WrightMolecular Biophysics Group, Institute of Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 7ZB, England.
Svetlana V AntonyukMolecular Biophysics Group, Institute of Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 7ZB, England.ORCID 0000-0002-2779-9946
Stephen P MuenchSchool of Biomedical Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, England.ORCID 0000-0001-6869-4414
S Samar HasnainMolecular Biophysics Group, Institute of Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 7ZB, England.ORCID 0000-0002-2854-4718
University of Liverpool · GBUniversity of Leeds · GB

Funding

Medical Research Council MRF-060-0002-RG-HASNAMotor Neurone Disease Association WRIGHT/OCT18/969-799
6 · The paper itself

Abstract

Solute carriers are a large class of transporters that play key roles in normal and disease physiology. Among the solute carriers, heteromeric amino-acid transporters (HATs) are unique in their quaternary structure. LAT1-CD98hc, a HAT, transports essential amino acids and drugs across the blood-brain barrier and into cancer cells. It is therefore an important target both biologically and therapeutically. During the course of this work, cryo-EM structures of LAT1-CD98hc in the inward-facing conformation and in either the substrate-bound or apo states were reported to 3.3-3.5 Å resolution [Yan et al. (2019), Nature (London), 568, 127-130]. Here, these structures are analyzed together with our lower resolution cryo-EM structure, and multibody 3D auto-refinement against single-particle cryo-EM data was used to characterize the dynamics of the interaction of CD98hc and LAT1. It is shown that the CD98hc ectodomain and the LAT1 extracellular surface share no substantial interface. This allows the CD98hc ectodomain to have a high degree of movement within the extracellular space. The functional implications of these aspects are discussed together with the structure determination.

Indexed as

Protein Interaction Domains and MotifsCryoelectron MicroscopyFusion Regulatory Protein 1, Heavy ChainHEK293 CellsHumansLarge Neutral Amino Acid-Transporter 1Models, MolecularFusion Regulatory Protein 1, Heavy ChainLarge Neutral Amino Acid-Transporter 1SLC3A2 protein, humanSLC7A5 protein, humanamino-acid transportersCD98hccryo-EMLAT1SLC3A2SLC7A5solute carrierstransporters

Identifiers

PMID31282475
PMCPMC7285653
OpenAlexW2953411699

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.