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Volume 272, Number 33, Issue of August 15, 1997 pp. 20793-20799
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Membrane Cofactor Protein (CD46) Is a Basolateral Protein That Is Not Endocytosed
IMPORTANCE OF THE TETRAPEPTIDE FTSL AT THE CARBOXYL TERMINUS

(Received for publication, April 30, 1997)

Andrea Maisner , Gert Zimmer , M. Kathryn Liszewski ^§ , Douglas M. Lublin ^¶ , John P. Atkinson ^§ and Georg Herrler

From the  Institut für Virologie, Philipps-Universität Marburg, D-35037 Marburg, Germany, the ^§ Division of Rheumatology, Department of Internal Medicine, and the ^¶ Division of Laboratory Medicine, Department of Pathology and Medicine, Washington University School of Medicine, St. Louis, Missouri 63110

Membrane cofactor protein (MCP) is a widely distributed complement regulatory protein that is expressed on the basolateral surface of polarized epithelial cells. The basolateral targeting of the BC1 isoform of MCP was analyzed by generating deletion mutants and point mutants within the cytoplasmic tail of 16 amino acids. A sequence of four amino acids, FTSL, was found to be indispensable for the basolateral transport of MCP. This tetrapeptide has two unique features compared with the targeting motifs of other basolateral proteins: (i) it contains a phenylalanine rather than a tyrosine at position 1; (ii) it is located at the very COOH-terminal end. Replacement of the phenylalanine or the leucine by an alanine resulted in a nonpolarized delivery to the cell surface. On the other hand, substitution of a tyrosine for the phenylalanine did not affect the basolateral transport of MCP. The latter mutant, however, was efficiently internalized, whereas the wild type protein was not subject to endocytosis. Our results indicate that the targeting signal YXX-large aliphatic that is involved in various sorting events has been modulated in MCP in such a way that it allows basolateral transport but not endocytosis.

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