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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.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Kobara A,Hiasa M,Matsumoto T,Otsuka M,Omote H,Moriyama Y

doi

10.1016/j.abb.2007.10.010

subject

Has Abstract

pub_date

2008-01-15 00:00:00

pages

195-9

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(07)00508-5

journal_volume

469

pub_type

杂志文章

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