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J. Biol. Chem., Vol. 283, Issue 7, 4177-4188, February 15, 2008

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Conserved Dimeric Subunit Stoichiometry of SLC26 Multifunctional Anion Exchangers^*

Silvia Detro-Dassen¹, Michael Schänzler¹, Heike Lauks, Ina Martin, Sonja Meyer zu Berstenhorst, Doreen Nothmann, Delany Torres-Salazar, Patricia Hidalgo, Günther Schmalzing²⁴, and Christoph Fahlke^¶34

From the Abteilung Molekulare Pharmakologie, Rheinisch-Westfälische Technische Hochschule Aachen University, Wendlingweg 2, Aachen 52074, the Institut für Neurophysiologie, Medizinische Hochschule Hannover, Carl-Neuberg-Strasse 1, Hannover 30625, and the ^¶Zentrum für Systemische Neurowissenschaften Hannover 30625, Hannover, Germany

The SLC26 gene family encodes multifunctional transport proteins in numerous tissues and organs. Some paralogs function as anion exchangers, others as anion channels, and one, prestin (SLC26A5), represents a membrane-bound motor protein in outer hair cells of the inner ear. At present, little is known about the molecular basis of this functional diversity. We studied the subunit stoichiometry of one bacterial, one teleost, and two mammalian SLC26 isoforms expressed in Xenopus laevis oocytes or in mammalian cells using blue native PAGE and chemical cross-linking. All tested SLC26s are assembled as dimers composed of two identical subunits. Co-expression of two mutant prestins with distinct voltage-dependent capacitances results in motor proteins with novel electrical properties, indicating that the two subunits do not function independently. Our results indicate that an evolutionarily conserved dimeric quaternary structure represents the native and functional state of SLC26 transporters.

Received for publication, June 14, 2007 , and in revised form, December 3, 2007.

^* This work was supported by the Deutsche Forschungsgemeinschaft (Grant FOR450 to P. H., G. S., and Ch. F.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1 and S2.

¹ Both authors contributed equally to this work as first authors.

⁴ Both authors contributed equally to this work as senior authors.

² To whom correspondence may be addressed. Tel.: 49-241-808-9130; Fax: 49-241-808-2433; E-mail: gschmalzing{at}ukaachen.de. ³ To whom correspondence may be addressed. Tel.: 49-511-532-2777; Fax: 49-511-532-2776; E-mail: fahlke.christoph{at}mh-hannover.de.

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