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J Biol Chem, Vol. 274, Issue 18, 12461-12467, April 30, 1999

The RGD Motif and the C-terminal Segment of Proprotein Convertase 1 Are Critical for Its Cellular Trafficking but Not for Its Intracellular Binding to Integrin alpha 5beta 1

Carole RovèreDagger , José Luis, Jean-Claude Lissitzkyparallel , Ajoy BasakDagger , Jacques Marvaldi, Michel ChrétienDagger , and Nabil G. SeidahDagger

From the Dagger  Laboratories of Biochemical and Molecular Neuroendocrinology, the Protein Engineering Network of Centres of Excellence, Clinical Research Institute of Montreal, University of Montreal, Montreal, Quebec H2W 1R7 Canada, the  Laboratoire de Biochimie Cellulaire CNRS-Unité Propre de Recherche de l'Enseignement Supérieur Associe'e 6032, Faculté de Pharmacie, 27 Blvd. Jean Moulin, 13385 Marseille, cedex 05, France, and parallel  INSERM U387 Hôpital Ste Marguerite, 270 Blvd. Ste Marguerite, 13009 Marseille, cedex 29, France

Cellular trafficking of subtilisin/kexin-like precursor convertases (PCs) may be regulated by a number of motifs, some of which are present within the P-domain and in the C-terminal sequence. Six of the seven known PCs contain a conserved RGD sequence within the P domain. In order to investigate the functional importance of this motif, we generated mutants of PC1 that contain a Myc tag epitope inserted between the prosegment and the catalytic subunit. Cellular expression of vaccinia virus recombinants revealed that this tag did not seem to influence the autocatalytic conversion of proPC1 into PC1 or its bioactivity. The two PC1 variants produced possess either the wild type RGD sequence or its RGE mutant. Stable transfectants of these variants in AtT20 cells revealed that similar to the wild type enzyme, PC1-RGD-Myc is sorted to secretory granules. In contrast, PC1-RGE-Myc exits the cell via the constitutive secretory pathway. In vitro, a 14-mer peptide spanning the RGD sequence of PC1, but not its RGE mutant, binds to cell surface vitronectin-binding integrins of Chinese hamster ovary cells. However, within the endoplasmic reticulum and in an RGD-independent fashion, integrin alpha 5beta 1 associates primarily with the zymogens proPC1, proPC1-Delta C (missing the C-terminal 137 residues), as well as proPC2. Thus, the observed discrimination between the secretion routes of PC1-RGD and PC1-RGE does not implicate integrins such as alpha 5beta 1.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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