A comparison between Skp2 and FOXO1 for their cytoplasmic localization by Akt1

Wang, Hongbo; Cui, Jinhua; Bauzon, Frederick; Zhu, Liang

doi:10.4161/cc.9.5.10916

Cited by 23 publications

(20 citation statements)

References 2 publications

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“…Notably, one research group reported that Akt could promote Skp2 translocation to the cytoplasm (12,48). A recent study revealed that Skp2 stimulated Akt activation in human breast cancer cells (49).…”

Section: Discussionmentioning

confidence: 99%

“…Recent studies have validated that S-phase kinase-associated protein 2 (Skp2) plays an essential role in the development of various human malignancies. Skp2 has been characterized to exhibit its oncogenic function via targeting of its substrates including p27 (7,8), p21 (9), p57 (10) and Forkhead box protein O1 (FOXO1) (11,12). Engineered mouse models revealed that conditional depletion of Skp2 in mice suppressed tumor growth in T cell lineage (13), B cell lineage (14), bone marrow (15), liver (16,17), breast (18), prostate (19) and skin cancer (20).…”

Section: Introductionmentioning

confidence: 99%

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Inhibition of Skp2 suppresses the proliferation and invasion of osteosarcoma cells

Ding

Han

et al. 2017

Oncology Reports

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Abstract. Osteosarcoma (OS) is a common bone tumor that mainly affects children and young adults. S-phase kinase-associated protein 2 (Skp2) has been characterized to play a critical oncogenic role in a variety of human malignancies. However, the biological function of Skp2 in OS remains largely obscure. In the present study, we elucidated the role of Skp2 in cell growth, cell cycle, apoptosis and migration in OS cells. We found that depletion of Skp2 inhibited cell growth in both MG-63 and SW 1353 cells. Moreover, we observed that depletion of Skp2 triggered cell apoptosis in two OS cell lines. Furthermore, downregulation of Skp2 induced cell cycle arrest in the G0/G1 phase in OS cells. Notably, our wound healing assay results revealed that inhibition of Skp2 suppressed cell migration in OS cells. Invariably, our western blot results demonstrated that depletion of Skp2 in OS cells inhibited activation of pAkt and increased p27 expression in OS cells, suggesting that Skp2 exerted its oncogenic function partly through the regulation of Akt and p27. Our findings revealed that targeting Skp2 could be a promising therapeutic strategy for the treatment of OS.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Inhibition of Skp2 suppresses the proliferation and invasion of osteosarcoma cells

Ding

Han

et al. 2017

Oncology Reports

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“…21 The FoxO subfamily of forkhead transcription factors are known regulators of these cellular processes as well, and their activity is regulated by PI3K/Akt. 22,23 Abrogation of PI3K/Akt signaling activates FoxO transcription factors, thus leading to cell cycle arrest and apoptosis. 22 On the contrary, phosphorylation of FoxO transcription factors by pAkt at Thr24, Ser256 and Ser319 curtails their ability to bind with DNA in the nucleus and, subsequent to complexation with 14-3-3 protein, they are exported out of the nucleus into the cytoplasm for degradation.…”

Section: Discussionmentioning

confidence: 99%

MicroRNA-143 is a critical regulator of cell cycle activity in stem cells with co-overexpression of Akt and angiopoietin-1 via transcriptional regulation of Erk5/cyclin D1 signaling

Lai¹,

Ashraf²,

Jiang³

et al. 2012

Cell Cycle

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“…Both direct phosphorylation by Akt (30,31) and p300-mediated acetylation (32) of specific residues within the nuclear localization signal of Skp2 have been identified and proposed to regulate the nuclear-cytoplasmic trafficking as well as the ubiquitylation activity of Skp2. Yet, these mechanisms remain controversial (33)(34)(35) and do not explain the effect of EBP50 on Skp2 (23). The experiments reported here support a novel mechanism for the Akt-dependent regulation of Skp2.…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of Ezrin-Radixin-Moesin-binding Phosphoprotein 50 (EBP50) by Akt Promotes Stability and Mitogenic Function of S-phase Kinase-associated Protein-2 (Skp2)

Song

Barrick²,

Mamonova³

et al. 2015

Journal of Biological Chemistry

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Background:The PDZ scaffolding protein EBP50 promotes Akt-dependent cell proliferation through the S-phase kinase associated protein-2 Skp2. Results: Akt phosphorylates threonine 156 of EBP50, allosterically promoting the binding of Skp2 to the first PDZ domain of EBP50. Conclusion:The interaction with EBP50 regulates the localization and stability of Skp2 and promotes cell proliferation. Significance: These studies define a regulatory mechanism contributing to Akt-dependent cell proliferation.

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A comparison between Skp2 and FOXO1 for their cytoplasmic localization by Akt1

Cited by 23 publications

References 2 publications

Inhibition of Skp2 suppresses the proliferation and invasion of osteosarcoma cells

Inhibition of Skp2 suppresses the proliferation and invasion of osteosarcoma cells

MicroRNA-143 is a critical regulator of cell cycle activity in stem cells with co-overexpression of Akt and angiopoietin-1 via transcriptional regulation of Erk5/cyclin D1 signaling

Phosphorylation of Ezrin-Radixin-Moesin-binding Phosphoprotein 50 (EBP50) by Akt Promotes Stability and Mitogenic Function of S-phase Kinase-associated Protein-2 (Skp2)

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