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Originally published In Press as doi:10.1074/jbc.M106882200 on October 22, 2001

J. Biol. Chem., Vol. 276, Issue 52, 49337-49342, December 28, 2001
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MAL Mediates Apical Transport of Secretory Proteins in Polarized Epithelial Madin-Darby Canine Kidney Cells*

Fernando Martín-BelmonteDagger §, Peter Arvan, and Miguel A. AlonsoDagger ||

From the Dagger  Centro de Biología Molecular "Severo Ochoa," Universidad Autónoma de Madrid and Consejo Superior de Investigaciones Científicas, Cantoblanco, 28049 Madrid, Spain and the  Department of Developmental and Molecular Biology and the Division of Endocrinology, Albert Einstein College of Medicine, Bronx, New York 10461

The MAL proteolipid is an integral membrane protein identified as a component of the raft machinery for apical sorting of membrane proteins in Madin-Darby canine kidney (MDCK) cells. Previous studies have implicated lipid rafts in the transport of exogenous thyroglobulin (Tg), the predominant secretory protein of thyroid epithelial cells, to the apical surface in MDCK cells. We have examined the secretion of recombinant Tg and gp80/clusterin, a major endogenous secretory protein not detected in Triton X-100 insoluble rafts, for the investigation of the involvement of MAL in the constitutive apical secretory pathway of MDCK cells. We show that MAL depletion impairs apical secretion of Tg and causes its accumulation in the Golgi. Cholesterol sequestration, which blocks apical secretion of Tg, did not alter the levels of MAL in rafts but created a block proximal to Tg entrance into rafts. Apical secretion of gp80/clusterin was also inhibited by elimination of endogenous MAL. Our results suggest a role for MAL in the transport of both endogenously and exogenously expressed apical secretory proteins in MDCK cells.

* This work was supported by grants from the Comunidad de Madrid (08.3/0025/2000), the Ministerio de Ciencia y Tecnología (PM99-0092), and the Fondo de Investigación Sanitaria (01/0085-01) (to M. A. A.) and by Grant DK40344 from the National Institutes of Health (to P. A.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Recipient of a postdoctoral fellowship from the Comunidad de Madrid.

|| To whom correspondence should be addressed. Tel.: 34-91-397-8037; Fax: 34-91-397-8087; E-mail: maalonso@cbm.uam.es.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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