A novel variant of mouse MATE-1 H+/organic cation antiporter with a long hydrophobic tail

Ayumi Kobara, Miki Hiasa, Takuya Matsumoto, Masato Otsuka, Hiroshi Omote, Yoshinori Moriyama

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)


Mammalian multidrug and toxic compound extrusion 1 (MATE1) are polyspecific H+-coupled exporters of organic cations (OCs) and responsible for excretion of metabolic waste products and xenobiotics. Here, we report a novel variant of mouse MATE1, mMATE1b, that has a long carboxyl terminal hydrophobic tail homologous to other MATE1 transporter proteins. Mouse MATE1b mediates tetraethylammonium (TEA) uptake with properties similar to that of mMATE1 and is localized in renal brush border membranes. Thus, mMATE1b is a functional variant of mMATE1 and seems to be the true counterpart to other MATE1 transporters.

Original languageEnglish
Pages (from-to)195-199
Number of pages5
JournalArchives of Biochemistry and Biophysics
Issue number2
Publication statusPublished - Jan 15 2008


  • MATE
  • Organic cation transporter
  • Xenobiotic exporter

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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