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Identification of Signal Peptide Peptidase, a Presenilin-Type Aspartic Protease
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.
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Activity-Based Profiling of Proteases
Sanman, L. E., & Bogyo, M. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035352 · Cited by 330
Lichtenthaler, S. F., Lemberg, M. K., & Fluhrer, R. (2018) · The EMBO Journal · doi:10.15252/embj.201899456 · Cited by 323
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Metadata
- Authors
- Weihofen, A., Binns, K., Lemberg, M. K., Ashman, K., & Martoglio, B.
- Venue
- Science
- Published
- 2002-06-21
- Volume
- 296
- Issue
- 5576
- Pages
- 2215-2218
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2033796514
- Cited by
- 532
- References
- 0
- FWCI
- 24.62
- Type
- journal article
- Language
- en
- Open access
- closed
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- Weihofen, A., Binns, K., Lemberg, M. K., Ashman, K., & Martoglio, B. (2002). Identification of Signal Peptide Peptidase, a Presenilin-Type Aspartic Protease. Science. https://doi.org/10.1126/science.1070925
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