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γ-Secretase Cleavage and Nuclear Localization of ErbB-4 Receptor Tyrosine Kinase
Abstract
ErbB-4 is a transmembrane receptor tyrosine kinase that regulates cell proliferation and differentiation. After binding of its ligand heregulin (HRG) or activation of protein kinase C (PKC) by 12- O -tetradecanoylphorbol-13-acetate (TPA), the ErbB-4 ectodomain is cleaved by a metalloprotease. We now report a subsequent cleavage by γ-secretase that releases the ErbB-4 intracellular domain from the membrane and facilitates its translocation to the nucleus. γ-Secretase cleavage was prevented by chemical inhibitors or a dominant negative presenilin. Inhibition of γ-secretase also prevented growth inhibition by HRG. γ-Secretase cleavage of ErbB-4 may represent another mechanism for receptor tyrosine kinase–mediated signaling.
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Metadata
- Authors
- Ni, C.-Y., Murphy, M. P., Golde, T. E., & Carpenter, G.
- Venue
- Science
- Published
- 2001-12-07
- Volume
- 294
- Issue
- 5549
- Pages
- 2179-2181
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2006257247
- Cited by
- 856
- References
- 2
- FWCI
- 27.41
- Type
- journal article
- Language
- en
- Open access
- closed
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- Ni, C.-Y., Murphy, M. P., Golde, T. E., & Carpenter, G. (2001). γ-Secretase Cleavage and Nuclear Localization of ErbB-4 Receptor Tyrosine Kinase. Science. https://doi.org/10.1126/science.1065412
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
