ATP13A3 is a major component of the enigmatic mammalian polyamine transport system.


Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
Historique:
received: 15 04 2020
revised: 27 11 2020
accepted: 11 12 2020
pubmed: 15 12 2020
medline: 19 8 2021
entrez: 14 12 2020
Statut: ppublish

Résumé

Polyamines, such as putrescine, spermidine, and spermine, are physiologically important polycations, but the transporters responsible for their uptake in mammalian cells remain poorly characterized. Here, we reveal a new component of the mammalian polyamine transport system using CHO-MG cells, a widely used model to study alternative polyamine uptake routes and characterize polyamine transport inhibitors for therapy. CHO-MG cells present polyamine uptake deficiency and resistance to a toxic polyamine biosynthesis inhibitor methylglyoxal bis-(guanylhydrazone) (MGBG), but the molecular defects responsible for these cellular characteristics remain unknown. By genome sequencing of CHO-MG cells, we identified mutations in an unexplored gene, ATP13A3, and found disturbed mRNA and protein expression. ATP13A3 encodes for an orphan P5B-ATPase (ATP13A3), a P-type transport ATPase that represents a candidate polyamine transporter. Interestingly, ATP13A3 complemented the putrescine transport deficiency and MGBG resistance of CHO-MG cells, whereas its knockdown in WT cells induced a CHO-MG phenotype demonstrated as a decrease in putrescine uptake and MGBG sensitivity. Taken together, our findings identify ATP13A3, which has been previously genetically linked with pulmonary arterial hypertension, as a major component of the mammalian polyamine transport system that confers sensitivity to MGBG.

Identifiants

pubmed: 33310703
pii: S0021-9258(20)00178-7
doi: 10.1074/jbc.RA120.013908
pmc: PMC7948421
pii:
doi:

Substances chimiques

Enzyme Inhibitors 0
Membrane Transport Proteins 0
Polyamines 0
Adenosine Triphosphatases EC 3.6.1.-
Mitoguazone OD5Q0L447W
Putrescine V10TVZ52E4

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

100182

Informations de copyright

Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.

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Auteurs

Norin Nabil Hamouda (NN)

Laboratory of Cellular Transport Systems, Department of Cellular and Molecular Medicine, KU Leuven, Leuven, Belgium.

Chris Van den Haute (C)

Laboratory for Neurobiology and Gene Therapy, Department of Neurosciences, KU Leuven, Leuven, Belgium; Leuven Viral Vector Core, KU Leuven, Leuven, Belgium.

Roeland Vanhoutte (R)

Laboratory of Chemical Biology, Department of Cellular and Molecular Medicine, KU Leuven, Leuven, Belgium.

Ragna Sannerud (R)

VIB-KU Leuven Laboratory of Membrane Trafficking, Department of Neurosciences, KU Leuven, Leuven, Belgium.

Mujahid Azfar (M)

Laboratory of Cellular Transport Systems, Department of Cellular and Molecular Medicine, KU Leuven, Leuven, Belgium.

Rupert Mayer (R)

Department for Biomolecular Medicine, VIB Center for Medical Biotechnology, VIB Proteomics Core, Ghent University, Ghent, Belgium.

Álvaro Cortés Calabuig (Á)

Genomics Core Leuven, KU Leuven, Leuven, Belgium.

Johannes V Swinnen (JV)

Laboratory of Lipid Metabolism and Cancer, Department of Oncology, LKI - Leuven Cancer Institute, KU Leuven, Leuven, Belgium.

Patrizia Agostinis (P)

Laboratory of Cell Death Research & Therapy, Department of Cellular and Molecular Medicine, KU Leuven, Leuven, Belgium; Department of Oncology, VIB-KU Leuven Center for Cancer Biology, KU Leuven, Leuven, Belgium.

Veerle Baekelandt (V)

Laboratory for Neurobiology and Gene Therapy, Department of Neurosciences, KU Leuven, Leuven, Belgium.

Wim Annaert (W)

VIB-KU Leuven Laboratory of Membrane Trafficking, Department of Neurosciences, KU Leuven, Leuven, Belgium.

Francis Impens (F)

Department for Biomolecular Medicine, VIB Center for Medical Biotechnology, VIB Proteomics Core, Ghent University, Ghent, Belgium.

Steven H L Verhelst (SHL)

Laboratory of Chemical Biology, Department of Cellular and Molecular Medicine, KU Leuven, Leuven, Belgium; Chemical Proteomics, Leibniz Institute for Analytical Sciences ISAS, Dortmund, Germany.

Jan Eggermont (J)

Laboratory of Cellular Transport Systems, Department of Cellular and Molecular Medicine, KU Leuven, Leuven, Belgium.

Shaun Martin (S)

Laboratory of Cellular Transport Systems, Department of Cellular and Molecular Medicine, KU Leuven, Leuven, Belgium.

Peter Vangheluwe (P)

Laboratory of Cellular Transport Systems, Department of Cellular and Molecular Medicine, KU Leuven, Leuven, Belgium. Electronic address: peter.vangheluwe@kuleuven.be.

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Classifications MeSH