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Science 21 June 2002:
Vol. 296. no. 5576, pp. 2215 - 2218
DOI: 10.1126/science.1070925
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Reports

Identification of Signal Peptide Peptidase, a Presenilin-Type Aspartic Protease

Andreas Weihofen,1 Kathleen Binns,2 Marius K. Lemberg,1 Keith Ashman,2 Bruno Martoglio1*

Signal peptide peptidase (SPP) catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein. In humans, SPP activity is required to generate signal sequence-derived human lymphocyte antigen-E epitopes that are recognized by the immune system, and to process hepatitis C virus core protein. We have identified human SPP as a polytopic membrane protein with sequence motifs characteristic of the presenilin-type aspartic proteases. SPP and potential eukaryotic homologs may represent another family of aspartic proteases that promote intramembrane proteolysis to release biologically important peptides.

1 Institute of Biochemistry, Swiss Federal Institute of Technology (ETH), ETH-Hoenggerberg, 8093 Zürich, Switzerland.
2 Samuel Lunenfeld Institute, Proteomics, 600 University Avenue, Toronto, Ontario M5G 1X5, Canada.
*   To whom correspondence should be addressed. E-mail: bruno.martoglio{at}bc.biol.ethz.ch

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