Signal sequences are the addresses of proteins destined for secretion. In eukaryotic cells, they mediate targeting to the endoplasmic reticulum membrane and insertion into the translocon. Thereafter, signal sequences are cleaved from the pre-protein and liberated into the endoplasmic reticulum membrane. We have recently reported that some liberated signal peptides are further processed by the intramembrane-cleaving aspartic protease signal peptide peptidase. Cleavage in the membrane-spanning portion of the signal peptide promotes the release of signal peptide fragments from the lipid bilayer. Typical processes that include intramembrane proteolysis is the regulatory or signalling function of cleavage products. Likewise, signal peptide fragments liberated upon intramembrane cleavage may promote such post-targeting functions in the cell.
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December 2003
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Conference Article|
December 01 2003
Intramembrane proteolysis and post-targeting functions of signal peptides
B. Martoglio
B. Martoglio
1
Institute of Biochemistry, Swiss Federal Institute of Technology (ETH), ETH-Hoenggerberg, 8093 Zurich, Switzerland
1e-mail bruno.martoglio@bc.biol.ethz.ch
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Publisher: Portland Press Ltd
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2003 Biochemical Society
2003
Biochem Soc Trans (2003) 31 (6): 1243–1247.
Citation
B. Martoglio; Intramembrane proteolysis and post-targeting functions of signal peptides. Biochem Soc Trans 1 December 2003; 31 (6): 1243–1247. doi: https://doi.org/10.1042/bst0311243
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