PKB/Akt mediates cell-cycle progression by phosphorylation of p27Kip1 at threonine 157 and modulation of its cellular localization

By I. Shin, F. Yakes, F. Rojo, Nah-Young Shin, Andrei V Bakin, J. Baselga, Carlos L. Arteaga. Nature Medicine, 2002

842 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/0549ef566c02b8c08eae74e2feb3ad8d35a58644

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. P. Pandolfi
2. T. Franke
3. Lewis C. Cantley
4. B. Manning
5. R. DePinho
6. David M. Sabatini
7. William C. Hahn
8. M. Moasser

In Oncology

1. Lewis C. Cantley
2. R. DePinho
3. William C. Hahn
4. C. Sherr
5. J. M. Roberts
6. D. Louis
7. M. Moasser
8. P. Pandolfi

Citations in the corpus

• Targeting PI3K/Akt signal transduction for cancer therapy (2021, background): “Studies have shown that the PI3K/Akt signaling pathway affects the cell cycle by modulating its downstream targets, thereby promoting the proliferation of tumor cells.(129) Akt phosphorylates cyclin-dependent kinase inhibitors and prevents p27 from translocating to the nucleus, thereby weakening its”
• Living with or without cyclins and cyclin-dependent kinases. (2004, background): “The AKT kinase controls the subcellular localization of Cip/Kip proteins as well (Liang et al. 2002; Shin et al. 2002; Viglietto et al. 2002), providing yet another avenue for cyclin E–Cdk2 regulation in response to extracellular cues.”
• Pten Dose Dictates Cancer Progression in the Prostate (2003, background): “It also remains to be resolved whether the reduction in p27Kip1 expression is also associated with its cytoplasmic relocalization, as previously reported in human breast cancer cells suffering AKT hyperactivation (Liang et al. 2002; Shin et al. 2002; Viglietto et al. 2002).”
• 14‐3‐3 suppresses the nuclear localization of threonine 157‐phosphorylated p27Kip1 (2004, background): “Phosphorylation of Thr157 of p27 by Akt also induces cytoplasmic localization of p27 in breast cancer (Liang et al, 2002; Shin et al, 2002; Viglietto et al, 2002), although the mechanism for this is currently unclear.”
• PI3K/Akt: getting it right matters (2008, positive): “Phosphorylation of p27Kip1 induces cytoplasmic localization and inhibition, similar to the regulation of p21Cip1/WAF1 (Liang et al., 2002; Shin et al., 2002).”
• The oncogene HER2: its signaling and transforming functions and its role in human cancer pathogenesis (2007, background): “Akt is activated in HER2-amplified breast cancers (reviewed above) and activated Akt phosphorylates p27 inhibiting its function by excluding it from the nucleus (Liang et al., 2002; Shin et al., 2002; Viglietto et al., 2002).”
• AKT/PKB signaling: navigating downstream. (2007, positive): “Several groups have independently found that Akt phosphorylates the p27Kip1 cyclin-dependent kinase inhibitor on T157 (Liang et al., 2002; Shin et al., 2002; Viglietto et al., 2002), and this leads to cytosolic sequestration via 14-3-3 binding (Sekimoto et al.”