The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
The Ubiquitin Ligase SCF Fbw7 Antagonizes Apoptotic JNK Signaling
Abstract
Jun N-terminal kinases (JNKs) are essential for neuronal microtubule assembly and apoptosis. Phosphorylation of the activating protein 1 (AP1) transcription factor c-Jun, at multiple sites within its transactivation domain, is required for JNK-induced neurotoxicity. We report that in neurons the stability of c-Jun is regulated by the E3 ligase SCF Fbw7 , which ubiquitinates phosphorylated c-Jun and facilitates c-Jun degradation. Fbw7 depletion resulted in accumulation of phosphorylated c-Jun, stimulation of AP1 activity, and neuronal apoptosis. SCF Fbw7 therefore antagonizes the apoptotic c-Jun–dependent effector arm of JNK signaling, allowing neurons to tolerate potentially neurotoxic JNK activity.
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Metadata
- Authors
- Nateri, A. S., Riera-Sans, L., Costa, C. D., & Behrens, A.
- Venue
- Science
- Published
- 2004-02-27
- Volume
- 303
- Issue
- 5662
- Pages
- 1374-1378
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2138779676
- Cited by
- 339
- References
- 22
- FWCI
- 9.40
- Type
- journal article
- Language
- en
- Open access
- closed
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- Nateri, A. S., Riera-Sans, L., Costa, C. D., & Behrens, A. (2004). The Ubiquitin Ligase SCF Fbw7 Antagonizes Apoptotic JNK Signaling. Science. https://doi.org/10.1126/science.1092880
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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