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 journalArticle

21 Citations (Scopus)

Abstract

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
Volume469
Issue number2
DOIs
Publication statusPublished - Jan 15 2008

Fingerprint

Antiporters
Poisons
Extrusion
Cations
Tail
Waste Products
Tetraethylammonium
Xenobiotics
Brushes
Microvilli
Membranes
Kidney
Proteins

Keywords

  • MATE
  • Organic cation transporter
  • Xenobiotic exporter

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

A novel variant of mouse MATE-1 H+/organic cation antiporter with a long hydrophobic tail. / Kobara, Ayumi; Hiasa, Miki; Matsumoto, Takuya; Otsuka, Masato; Omote, Hiroshi; Moriyama, Yoshinori.

In: Archives of Biochemistry and Biophysics, Vol. 469, No. 2, 15.01.2008, p. 195-199.

Research output: Contribution to journalArticle

Kobara, Ayumi ; Hiasa, Miki ; Matsumoto, Takuya ; Otsuka, Masato ; Omote, Hiroshi ; Moriyama, Yoshinori. / A novel variant of mouse MATE-1 H+/organic cation antiporter with a long hydrophobic tail. In: Archives of Biochemistry and Biophysics. 2008 ; Vol. 469, No. 2. pp. 195-199.
@article{72214ad2c516423383f4cd05465886fe,
title = "A novel variant of mouse MATE-1 H+/organic cation antiporter with a long hydrophobic tail",
abstract = "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.",
keywords = "MATE, Organic cation transporter, Xenobiotic exporter",
author = "Ayumi Kobara and Miki Hiasa and Takuya Matsumoto and Masato Otsuka and Hiroshi Omote and Yoshinori Moriyama",
year = "2008",
month = "1",
day = "15",
doi = "10.1016/j.abb.2007.10.010",
language = "English",
volume = "469",
pages = "195--199",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - A novel variant of mouse MATE-1 H+/organic cation antiporter with a long hydrophobic tail

AU - Kobara, Ayumi

AU - Hiasa, Miki

AU - Matsumoto, Takuya

AU - Otsuka, Masato

AU - Omote, Hiroshi

AU - Moriyama, Yoshinori

PY - 2008/1/15

Y1 - 2008/1/15

N2 - 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.

AB - 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.

KW - MATE

KW - Organic cation transporter

KW - Xenobiotic exporter

UR - http://www.scopus.com/inward/record.url?scp=37349059967&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=37349059967&partnerID=8YFLogxK

U2 - 10.1016/j.abb.2007.10.010

DO - 10.1016/j.abb.2007.10.010

M3 - Article

C2 - 17983590

AN - SCOPUS:37349059967

VL - 469

SP - 195

EP - 199

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 2

ER -