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Requirements for Presenilin-Dependent Cleavage of Notch and Other Transmembrane Proteins
Open accessAbstract
Ligand binding to receptors of the LIN-12/Notch family causes at least two proteolytic cleavages: one between the extracellular and transmembrane domains, and the other within the transmembrane domain. The transmembrane cleavage depends on Presenilin, a protein also required for transmembrane cleavage of beta-APP. Here, we have assayed the substrate requirements for Presenilin-dependent processing of Notch and other type I transmembrane proteins in vivo. We find that the Presenilin-dependent cleavage does not depend critically on the recognition of particular sequences in these proteins but rather on the size of the extracellular domain: the smaller the size, the greater the efficiency of cleavage. Hence, Notch, beta-APP, and perhaps other proteins may be targeted for Presenilin-mediated transmembrane cleavage by upstream processing events that sever the extracellular domain from the rest of the protein.
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Cites
Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876
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Metadata
- Authors
- Struhl, G., & Adachi, A.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2000-09
- Volume
- 6
- Issue
- 3
- Pages
- 625-636
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2063733034
- Cited by
- 423
- References
- 1
- FWCI
- 17.01
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Struhl, G., & Adachi, A. (2000). Requirements for Presenilin-Dependent Cleavage of Notch and Other Transmembrane Proteins. Molecular Cell. https://doi.org/10.1016/s1097-2765(00)00061-7
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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
