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Originally published In Press as doi:10.1074/jbc.M100857200 on April 9, 2001

J. Biol. Chem., Vol. 276, Issue 25, 22788-22796, June 22, 2001
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Activation and Functional Characterization of the Mosaic Receptor SorLA/LR11*

Linda JacobsenDagger , Peder Madsen, Christian Jacobsen, Morten S. Nielsen, Jørgen Gliemann§, and Claus M. Petersen

From the Department of Medical Biochemistry, University of Aarhus, DK-8000, Aarhus C, Denmark

We previously isolated and sequenced the ~250-kDa type 1 receptor sorLA/LR11, a mosaic protein with elements characterizing the Vps10p domain receptor family as well as the low density lipoprotein receptor family. The N terminus of the Vps10p domain comprises a consensus sequence for cleavage by furin (50RRKR53) that precedes a truncation found in sorLA isolated from human brain. Here we show that sorLA, like sortilin-1/neurotensin receptor-3, whose lumenal domain consists of a Vps10p domain only, is synthesized as a proreceptor that is cleaved by furin in late Golgi compartments. We show that the truncation conditions the Vps10p domain for propeptide inhibitable binding of neuropeptides and the receptor-associated protein. We further demonstrate that avid binding of the receptor-associated protein, apolipoprotein E, and lipoprotein lipase not inhibited by propeptide occurs to sites located in other lumenal domains. In transfected cells, about 10% of full-length sorLA were expressed on the cell surface capable of mediating endocytosis. However, the major pool of receptors was found in late Golgi compartments, suggesting possible interaction with newly synthesized ligands. The results show that sorLA, following activation by truncation, binds multiple ligands and may mediate both endocytosis and sorting.

* This work was supported by grants from the Danish Medical Research Council, the Danish Biotechnology Program, the Novo Nordic Foundation, and the Aarhus University Research Foundation.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.

Dagger Present address: Faculty of Biology, Vrije University, de Boelelaan 1087, 1081 HV Amsterdam, The Netherlands.

§ To whom correspondence should be addressed: Dept. of Medical Biochemistry, University of Aarhus, Ole Worms Allé, Bldg. 170, DK-8000 Aarhus C, Denmark. Tel.: 45-89-422880; Fax: 45-86-131160; E-mail: jg@biokemi.au.dk.

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