PKB/Akt phosphorylates p27, impairs nuclear import of p27 and opposes p27-mediated G1 arrest

By Jiyong Liang, Judit Zubovitz, T. Petrocelli, R. Kotchetkov, M. Connor, Kathy Han, Jin-Hwa Lee, Sandra Ciarallo, C. Catzavelos, R. Beniston and 2 more. Nature Medicine, 2002

1,010 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/83de671f5f0d80566b5b8fec8104487707507cad

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Citations in the corpus

The energy sensing LKB1–AMPK pathway regulates p27kip1 phosphorylation mediating the decision to enter autophagy or apoptosis (2007, methodology): “YFP–p27 T198A and YFP–p27 T198D were generated by replacing respective amino acid residues of YFP–p27 (ref”
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).”
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.”
CDK inhibitors: cell cycle regulators and beyond. (2008, neutral): “…Akt or Thr-198 by PKB/Akt or p90 ribosomal S6-kinase (p90RSK) causes retention of p27 in the cytoplasm by promoting the association of p27 with 14-3-3, which prevents p27 from interacting with importin a and transport in the nucleus (Fujita et al., 2003; Liang et al., 2002; Sekimoto et al., 2004).”
Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis (2006, background): “These substrates include the cell-cycle inhibitor p27 (also known as KIP1), the forkhead box transcription factors (FOXO), glycogen synthase kinase 3 (GSK3), serum- and glucocorticoid-induced kinase 1 ( SGK1 ) and tuberous sclerosis complex 2 ( TSC2”
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.”