The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Akt-dependent Phosphorylation of p27Kip1Promotes Binding to 14-3-3 and Cytoplasmic Localization
Open accessAbstract
In many human cancers, the cyclin-dependent kinase inhibitor p27(Kip1) is expressed at low or undetectable levels. The decreased p27(Kip1) expression allows cyclin-dependent kinase activity to cause cells to enter into S phase and correlates with poor patient survival. Inhibition of serine/threonine kinase Akt signaling by some pharmacological agents or by PTEN induces G(1) arrest, in part by up-regulating p27(Kip1). However, the role of Akt-dependent phosphorylation in p27(Kip1) regulation is not clear. Here, we show that Akt bound directly to and phosphorylated p27(Kip1). Screening p27(Kip1) phosphorylation sites identified the COOH-terminal Thr(198) residue as a novel site. Further analysis revealed that 14-3-3 proteins bound to p27(Kip1) through Thr(198) only when it was phosphorylated by Akt. Although Akt also phosphorylated p27(Kip1) at Ser(10) and Thr(187), these two sites were not involved in the binding to 14-3-3 proteins. p27(Kip1) phosphorylated at Thr(198) exists only in the cytoplasm. Therefore, Akt promotes cell-cycle progression through the mechanisms of phosphorylation-dependent 14-3-3 binding to p27(Kip1) and cytoplasmic localization.
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Cited by
The Ras-ERK and PI3K-mTOR pathways: cross-talk and compensation
Mendoza, M. C., Er, E. E., & Blenis, J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.03.006 · Cited by 1,817
The Cdk inhibitor p27 in human cancer: prognostic potential and relevance to anticancer therapy
Chu, I. M., Hengst, L., & Slingerland, J. M. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2347 · Cited by 990
Oncogenic PI3K deregulates transcription and translation
Bader, A. G., Kang, S., Zhao, L., & Vogt, P. K. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1753 · Cited by 798
FoxO transcription factors; Regulation by AKT and 14-3-3 proteins
Tzivion, G., Dobson, M., & Ramakrishnan, G. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.06.002 · Cited by 728
The PI3K/AKT/mTOR interactive pathway
Ersahin, T., Tuncbag, N., & Cetin-Atalay, R. (2015) · Molecular BioSystems · doi:10.1039/c5mb00101c · Cited by 683
Metadata
- Authors
- Fujita, N., Sato, S., Katayama, K., & Tsuruo, T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-08
- Volume
- 277
- Issue
- 32
- Pages
- 28706-28713
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2111613650
- Cited by
- 358
- References
- 45
- FWCI
- 8.53
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Akt-dependent Phosphorylation of p27Kip1Promotes Binding to 14-3-3 and Cytoplasmic Localization. https://app.cochat.ai/papers/10.1074/jbc.m203668200
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- Fujita, N., Sato, S., Katayama, K., & Tsuruo, T. (2002). Akt-dependent Phosphorylation of p27Kip1Promotes Binding to 14-3-3 and Cytoplasmic Localization. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m203668200
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