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Originally published In Press as doi:10.1074/jbc.M004757200 on September 26, 2000

J. Biol. Chem., Vol. 275, Issue 51, 40337-40343, December 22, 2000
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A Predicted alpha -Helix Mediates Targeting of the Proprotein Convertase PC1 to the Regulated Secretory Pathway*

Isabelle JutrasDagger §, Nabil G. Seidah, and Timothy L. ReudelhuberDagger ||

From the Dagger  Laboratories of Molecular Biochemistry of Hypertension and  Biochemical Neuroendocrinology, Clinical Research Institute of Montreal, Montreal, Quebec H2W 1R7, Canada

The proprotein convertase PC1 is a protease whose activity is largely confined to the dense core secretory granules of neuroendocrine cells. Efficient processing of PC1 substrates in granules requires a mechanism that will both limit the activity of the enzyme to these organelles and promote its targeting to the nascent secretory granules. In the current study, we provide evidence that targeting of PC1 to secretory granules is mediated by alpha -helical structures in its C-terminal tail and, at least in part, is dependent on interactions with specific components of the secretory granule membrane.

* This work was supported in part by grants from the Medical Research Council of Canada.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 graduate scholarship from the Heart and Stroke Foundation of Canada.

|| To whom correspondence should be addressed: Laboratory of Molecular Biochemistry of Hypertension, IRCM, 110 Pine Ave. West, Montreal, Quebec H2W 1R7, Canada. Tel.: 514- 987-5716; Fax: 514-987-5717; E-mail: reudelt@ircm.qc.ca.

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