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M101703200v1
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Papers In Press, published online ahead of print May 7, 2001
J. Biol. Chem, 10.1074/jbc.M101703200
Submitted on February 23, 2001
Revised on April 27, 2001
Accepted on May 7, 2001

Alternative splicing regulates the endoplasmic reticulum localization or secretion of soluble secreted endopeptidase (SEP)

Sunu Budhi Raharjo, Noriaki Emoto, Koji Ikeda, Ryuichiro Sato, Mitsuhiro Yokoyama, and Masafumi Matsuo

Department of Internal Medicine, Kobe University Graduate School of Medicine, Kobe, Hyogo 6500017

Corresponding Author: emoto{at}med.kobe-u.ac.jp

A subfamily of zinc metalloproteases, represented by neutral endopeptidase 24.11 and endothelin converting enzyme, is involved in the metabolism of a variety of biologically active peptides. Recently, we cloned and characterized a novel member of this metalloprotease family, termed soluble secreted endopeptidase (SEP), which hydrolyzes many vasoactive peptides. Here we report that alternative splicing of the mouse SEP gene generates two polypeptides, SEP-delta and SEP. After synthesis, both isoforms are inserted into the endoplasmic reticulum (ER) as type II membrane proteins. SEP-delta then becomes an ER resident, whereas SEP, which differs by only the presence of 23 residues at the beginning of its luminal domain, is proteolytically cleaved by membrane secretase(s) in the ER and is transported into the extracellular compartment. Analysis of the chimeric proteins between SEP-delta and bovine endothelin converting enzyme-1b (bECE-1b) demonstrated that the retention of SEP-delta in the ER is mediated by the luminal domain. In addition, the dissection of the chimeric bECE-1b/SEP insertion showed that its insertion domain is obviously responsible for its secretion. A series of mutagenesis in this region revealed that the minimal requirement for cleavage was found to be a WDERTVV motif. Our results suggest that the unique subcellular localization and secretion of SEP proteins provide a novel model of protein trafficking within the secretory pathway.


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