Proteomics

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


ABSTRACT: Polyamines, including putrescine (PUT), spermidine (SPD) and spermine (SPM), are abundant polycations supporting various cellular functions. Their cellular content is tightly controlled by biosynthesis, degradation and uptake or export via the polyamine transport system (PTS). However, the mammalian PTS remains poorly characterized. Mutated Chinese hamster ovary cells, CHO-MG, are frequently used to study the PTS owing to their phenotype of reduced polyamine uptake and resistance to methylglyoxal bis-(guanylhydrazone) (MGBG), a toxic polyamine biosynthesis inhibitor. Yet, the underlying genetic defect remains enigmatic. We recently proved that the P5B-type ATPase, ATP13A2, is a polyamine transporter and here, we analyzed whether the P5B-type ATPases are deficient in CHO-MG. Label-free shogun proteomics found that ATP13A3 expression is reduced in CHO-MG. Mutations in the ATP13A3 gene were found to critically disturb the protein sequence. Interestingly, depleting ATP13A3 in the wild-type CHO cells induced a CHO-MG phenotype, whereas its complementation in CHO-MG rescued the phenotype. Together, we demonstrate that defective ATP13A3 contributes to the CHO-MG phenotype, designating ATP13A3 as a new member of the mammalian PTS that may partially overlap in function with ATP13A2.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Cricetulus Griseus (chinese Hamster) (cricetulus Barabensis Griseus)

TISSUE(S): Epithelial Cell, Cell Culture

SUBMITTER: Rupert Mayer  

LAB HEAD: Peter Vangheluwe

PROVIDER: PXD020559 | Pride | 2020-12-09

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
ATP13A1.fasta Fasta
ATP13A2.fasta Fasta
ATP13A3.fasta Fasta
ATP13A4.fasta Fasta
CHO_20190905_23885seq.fasta Fasta
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Publications


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 poly  ...[more]

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