Evidence map›Paper›PMID 36028562›Full record

ArticleScientific reports2022

N-glycosylation is crucial for trafficking and stability of SLC3A2 (CD98).

Lara Console, Mariafrancesca Scalise, Simona Salerno, Raffaella Scanga, Deborah Giudice, Loredana De Bartolo, Annamaria Tonazzi, Cesare Indiveri

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. 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
3.8field-weighted citation impact, top 7% 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, 29 citations in OpenAlex.

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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 at 4 institutions in 1 country.

Lara Console *Department DiBEST (Biologia, Ecologia, Scienze Della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria, Via Bucci 4C, 87036, Arcavacata di Rende, Italy.
Mariafrancesca Scalise *Department DiBEST (Biologia, Ecologia, Scienze Della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria, Via Bucci 4C, 87036, Arcavacata di Rende, Italy.
Simona SalernoCNR Institute on Membrane Technology, National Research Council of Italy (CNR-ITM), Via P. Bucci, cubo 17/C, 87036, Rende, Italy.
Raffaella ScangaDepartment DiBEST (Biologia, Ecologia, Scienze Della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria, Via Bucci 4C, 87036, Arcavacata di Rende, Italy.
Deborah GiudiceDepartment DiBEST (Biologia, Ecologia, Scienze Della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria, Via Bucci 4C, 87036, Arcavacata di Rende, Italy.
Loredana De BartoloCNR Institute on Membrane Technology, National Research Council of Italy (CNR-ITM), Via P. Bucci, cubo 17/C, 87036, Rende, Italy.
Annamaria TonazziCNR Institute of Biomembranes, Bioenergetics and Molecular Biotechnologies (IBIOM), Via Amendola 122/O, 70126, Bari, Italy.
Cesare IndiveriDepartment DiBEST (Biologia, Ecologia, Scienze Della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria, Via Bucci 4C, 87036, Arcavacata di Rende, Italy. cesare.indiveri@unical.it.
University of Calabria · ITInstitute of Biomembranes, Bioenergetics and Molecular Biotechnologies · ITInstitute on Membrane Technology · ITNational Research Council · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The type II glycoprotein CD98 (SLC3A2) is a membrane protein with pleiotropic roles in cells, ranging from modulation of inflammatory processes, host-pathogen interactions to association with membrane transporters of the SLC7 family. The recent resolution of CD98 structure in complex with LAT1 showed that four Asn residues, N365, N381, N424, N506, harbour N-glycosylation moieties. Then, the role of N-glycosylation on CD98 trafficking and stability was investigated by combining bioinformatics, site-directed mutagenesis and cell biology approach. Single, double, triple and quadruple mutants of the four Asn exhibited altered electrophoretic mobility, with apparent molecular masses from 95 to 70 kDa. The quadruple mutant displayed a single band of 70 kDa corresponding to the unglycosylated protein. The presence in the membrane and the trafficking of CD98 were evaluated by a biotinylation assay and a brefeldin assay, respectively. Taken together, the results highlighted that the quadruple mutation severely impaired both the stability and the trafficking of CD98 to the plasma membrane. The decreased presence of CD98 at the plasma membrane, correlated with a lower presence of LAT1 (SLC7A5) and its transport activity. This finding opens new perspectives for human therapy. Indeed, the inhibition of CD98 trafficking would act synergistically with LAT1 inhibitors that are under clinical trial for anticancer therapy.

Indexed as

Large Neutral Amino Acid-Transporter 1Membrane Transport ProteinsCell MembraneFusion Regulatory Protein 1, Heavy ChainGlycosylationHumansMutagenesis, Site-DirectedFusion Regulatory Protein 1, Heavy ChainLarge Neutral Amino Acid-Transporter 1Membrane Transport ProteinsSLC3A2 protein, human

Identifiers

PMID36028562
PMCPMC9418156
OpenAlexW4293109550

What OpenQuestion holds

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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.