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J. Biol. Chem., Vol. 280, Issue 52, 42636-42643, December 30, 2005

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A Novel Type of Detergent-resistant Membranes May Contribute to an Early Protein Sorting Event in Epithelial Cells^*

Marwan Alfalah, Gabi Wetzel, Ina Fischer, Roger Busche, Erwin E. Sterchi, Klaus-Peter Zimmer¶, Hans-Peter Sallmann, and Hassan Y. Naim1

From the Department of Physiological Chemistry, School of Veterinary Medicine, D-30559 Hannover, Germany, Institute of Biochemistry and Molecular Biology, University of Bern, CH-3012 Bern, Switzerland, and the ^¶Children's Hospital of the University of Münster, D48149 Münster, Germany

One sorting mechanism of apical and basolateral proteins in epithelial cells is based on their solubility profiles with Triton X-100. Nevertheless, apical proteins themselves are also segregated beyond the trans-Golgi network by virtue of their association or nonassociation with cholesterol/sphingolipid-rich microdomains (Jacob, R., and Naim, H. Y. (2001) Curr. Biol. 11, 1444–1450). Therefore, extractability with Triton X-100 does not constitute an absolute criterion of protein sorting. Here, we investigate the solubility patterns of apical and basolateral proteins with other detergents and demonstrate that the mild detergent Tween 20 is adequate to discriminate between apical and basolateral proteins during early stages in their biosynthesis. Although the mannose-rich forms of the apical proteins sucrase-isomaltase, lactase-phlorizin hydrolase, aminopeptidase N, and dipeptidylpeptidase IV reveal similar solubility profiles comprising soluble and nonsoluble fractions, the basolateral proteins, vesicular stomatitis virus G protein, major histocompatibility complex class I, and CD46 are entirely soluble with this detergent. The insoluble Tween 20 membranes are enriched in phosphatidylinositol and phosphatidylglycerol compatible with their synthesis in the endoplasmic reticulum and the existence of a novel class of detergent-resistant membranes. The association of the mannose-rich biosynthetic forms of the apical proteins, sucraseisomaltase, lactase-phlorizin hydrolase, aminopeptidase N, and dipeptidylpeptidase IV with the Tween 20-resistant membranes suggests an early polarized sorting mechanism prior to maturation in the Golgi apparatus.

Received for publication, May 31, 2005 , and in revised form, October 13, 2005.

^* This work was supported by Deutsche Forschungsgemeinschaft Grant Na 331/1-4 and Sonderforschungsbereich Grant 621 (to H. Y. N.) and by Swiss National Foundation Grant 3100A0-100772 (to E. E. S.). 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 figures.

¹ To whom correspondence should be addressed: Dept. of Physiological Chemistry, University of Veterinary Medicine Hannover, Bünteweg 17, D-30559 Hannover, Germany. Tel.: 49-511-953-8780; Fax: 49-511-953-8585; E-mail: hassan.naim{at}tiho-hannover.de.

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