The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport
Open accessAbstract
14-3-3 proteins regulate the cell cycle and prevent apoptosis by controlling the nuclear and cytoplasmic distribution of signaling molecules with which they interact. Although the majority of 14-3-3 molecules are present in the cytoplasm, we show here that in the absence of bound ligands 14-3-3 homes to the nucleus. We demonstrate that phosphorylation of one important 14-3-3 binding molecule, the transcription factor FKHRL1, at the 14-3-3 binding site occurs within the nucleus immediately before FKHRL1 relocalization to the cytoplasm. We show that the leucine-rich region within the COOH-terminal α-helix of 14-3-3, which had been proposed to function as a nuclear export signal (NES), instead functions globally in ligand binding and does not directly mediate nuclear transport. Efficient nuclear export of FKHRL1 requires both intrinsic NES sequences within FKHRL1 and phosphorylation/14-3-3 binding. Finally, we present evidence that phosphorylation/14-3-3 binding may also prevent FKHRL1 nuclear reimport. These results indicate that 14-3-3 can mediate the relocalization of nuclear ligands by several mechanisms that ensure complete sequestration of the bound 14-3-3 complex in the cytoplasm.
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Cites
Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor
Brunet, A., Bonni, A., Zigmond, M. J., Lin, M. Z., Juo, P., Hu, L. S., Anderson, M. J., Arden, K. C., Blenis, J., & Greenberg, M. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80595-4 · Cited by 5,594
Self-citationCRM1 Is an Export Receptor for Leucine-Rich Nuclear Export Signals
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The Structural Basis for 14-3-3:Phosphopeptide Binding Specificity
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Self-citation14-3-3 Proteins: Structure, Function, and Regulation
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Interaction of 14-3-3 with Signaling Proteins Is Mediated by the Recognition of Phosphoserine
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Is a p53-Regulated Inhibitor of G2/M Progression
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CRM1 is responsible for intracellular transport mediated by the nuclear export signal
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The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors
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Huang, E. J., & Reichardt, L. F. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161629 · Cited by 2,537
Transcriptional regulation by calcium, calcineurin, and NFAT
Hogan, P. G., Chen, L., Nardone, J., & Rao, A. (2003) · Genes & Development · doi:10.1101/gad.1102703 · Cited by 1,991
Calnan, D. R., & Brunet, A. (2008) · Oncogene · doi:10.1038/onc.2008.21 · Cited by 1,170
Self-citationMetabolic Regulation of Hematopoietic Stem Cells in the Hypoxic Niche
Suda, T., Takubo, K., & Semenza, G. L. (2011) · Cell Stem Cell · doi:10.1016/j.stem.2011.09.010 · Cited by 844
Redox regulation of FoxO transcription factors
Klotz, L.-O., Sánchez-Ramos, C., Prieto-Arroyo, I., Urbánek, P., Steinbrenner, H., & Monsalve, M. (2015) · Redox Biology · doi:10.1016/j.redox.2015.06.019 · Cited by 747
Metadata
- Authors
- Brunet, A., Kanai, F., Stehn, J., Xu, J., Sarbassova, D., Frangioni, J. V., Dalal, S. N., DeCaprio, J. A., Greenberg, M. E., & Yaffe, M. B.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2002-02-25
- Volume
- 156
- Issue
- 5
- Pages
- 817-828
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2096576561
- Cited by
- 561
- References
- 37
- FWCI
- 10.04
- Type
- journal article
- Language
- en
- Open access
- green
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- Brunet, A., Kanai, F., Stehn, J., Xu, J., Sarbassova, D., Frangioni, J. V., Dalal, S. N., DeCaprio, J. A., Greenberg, M. E., & Yaffe, M. B. (2002). 14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport. The Journal of Cell Biology. https://doi.org/10.1083/jcb.200112059
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