Report

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

Science  21 Jun 2002:
Vol. 296, Issue 5576, pp. 2215-2218
DOI: 10.1126/science.1070925

You are currently viewing the abstract.

View Full Text
As a service to the community, AAAS/Science has made this article free with registration.

Abstract

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.

  • * To whom correspondence should be addressed. E-mail: bruno.martoglio{at}bc.biol.ethz.ch

View Full Text

Cited By...