Dual Transport Properties of Anion Exchanger 1 THE SAME TRANSMEMBRANE SEGMENT IS INVOLVED IN ANION EXCHANGE AND IN A CATION LEAK

被引：13

作者：

Barneaud-Rocca, Damien ^{[1
]}

Borgese, Franck ^{[1
]}

Guizouarn, Helene ^{[1
]}

机构：

[1] Univ Nice, IBDC, Ctr Natl Rech Sci, UMR6543, F-06108 Nice 2, France

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2011年 / 286卷 / 11期

关键词：

RENAL TUBULAR-ACIDOSIS; CELL-VOLUME REGULATION; SCANNING MUTAGENESIS; CHLORIDE CHANNEL; MEMBRANE DOMAIN; POINT MUTATIONS; BAND-3; PROTEIN; IONIC-STRENGTH; HUMAN AE1; ERYTHROCYTE;

D O I：

10.1074/jbc.M110.166819

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Previous results suggested that specific point mutations in human anion exchanger 1 (AE1) convert the electroneutral anion exchanger into a monovalent cation conductance. In the present study, the transport site for anion exchange and for the cation leak has been studied by cysteine scanning mutagenesis and sulfhydryl reagent chemistry. Moreover, the role of some highly conserved amino acids within members of the SLC4 family to which AE1 belongs has been assessed in AE1 transport properties. The results suggest that the same transport site within the AE1 spanning domain is involved in anion exchange or in cation transport. A functioning mechanism for this transport site is proposed according to transport properties of the different studied point mutations of AE1.

引用

页码：8909 / 8916

页数：8

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