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Originally published In Press as doi:10.1074/jbc.M006758200 on August 29, 2000

J. Biol. Chem., Vol. 275, Issue 49, 38842-38847, December 8, 2000
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Binding of BiP to the Processing Enzyme Lymphoma Proprotein Convertase Prevents Aggregation, but Slows Down Maturation*

John W. M. CreemersDagger §, Jan-Willem H. P. van de LooDagger , Evelyn PletsDagger , Linda M. Hendershot, and Wim J. M. Van de VenDagger

From the Dagger  Laboratory for Molecular Oncology, Center for Human Genetics, University of Leuven and Flanders Interuniversity Institute for Biotechnology, Herestraat 49, 3000 Leuven, Belgium and the  Department of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105

Lymphoma proprotein convertase (LPC) is a subtilisin-like serine protease of the mammalian proprotein convertase family. It is synthesized as an inactive precursor protein, and propeptide cleavage occurs via intramolecular cleavage in the endoplasmic reticulum. In contrast to other convertases like furin and proprotein convertase-1, propeptide cleavage occurs slowly. Also, both a glycosylated and an unglycosylated precursor are detected. Here we demonstrate that the unglycosylated precursor form of LPC is localized in the cytosol due to the absence of a signal peptide. Using a reducible cross-linker, we found that glycosylated pro-LPC is associated with the molecular chaperone BiP. In addition, we show that pro-LPC is prone to aggregation and forms large complexes linked via interchain disulfide bonds. BiP is associated mainly with non-aggregated pro-LPC and pro-LPC dimers and trimers, suggesting that BiP prevents aggregation. Overexpression of wild-type BiP or a dominant-negative BiP ATPase mutant resulted in reduced processing of pro-LPC. Taken together, these results suggest that binding of BiP to pro-LPC prevents aggregation, but results in slower maturation.

* This work was supported in part by the "Geconcerteerde Onderzoeksacties" 1997-2001.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.

§ Postdoctoral Fellow of the "Fonds voor Wetenschappelijk Onderzoek, Vlaanderen." To whom correspondence should be addressed. Tel.: 32-16-346082; Fax: 32-16-346073; E-mail: john.creemers@med.kuleuven.ac.be.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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