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Miranda, Fabrizio; Mannion, David; Liu, Shujuan; Zheng, Yiyan; Mangala, Lingegowda S.; Redondo, Clara; Herrero-Gonzalez, Sandra; Xu, Ruoyan; Taylor, Charlotte; Chedom, Donatien Fotso; Carrami, Eli M.; Albukhari, Ashwag; Jiang, Dahai; Pradeep, Sunila; Rodriguez-Aguayo, Cristian; Lopez-Berestein, Gabriel; Salah, Eidarus; Abdul Azeez, Kamal R.; Elkins, Jonathan M.; Campo, Leticia; Myers, Kevin A.; Klotz, Daniel; Bivona, Serena; Dhar, Sunanda; Bast, Robert C.; Saya, Hideyuki; Choi, Hwan Geun; Gray, Nathanael S.; Fischer, Roman; Kessler, Benedikt M.; Yau, Christopher; Sood, Anil K.; Motohara, Takeshi; Knapp, Stefan; Ahmed, Ahmed Ashour
Cancer cell, 08/2016, Letnik: 30, Številka: 2Journal Article
The adipocyte-rich microenvironment forms a niche for ovarian cancer metastasis, but the mechanisms driving this process are incompletely understood. Here we show that salt-inducible kinase 2 (SIK2) is overexpressed in adipocyte-rich metastatic deposits compared with ovarian primary lesions. Overexpression of SIK2 in ovarian cancer cells promotes abdominal metastasis while SIK2 depletion prevents metastasis in vivo. Importantly, adipocytes induce calcium-dependent activation and autophosphorylation of SIK2. Activated SIK2 plays a dual role in augmenting AMPK-induced phosphorylation of acetyl-CoA carboxylase and in activating the PI3K/AKT pathway through p85α-S154 phosphorylation. These findings identify SIK2 at the apex of the adipocyte-induced signaling cascades in cancer cells and make a compelling case for targeting SIK2 for therapy in ovarian cancer. Display omitted •SIK2 is highly expressed in adipocyte-rich metastases•SIK2 is required for adipocyte-induced proliferation of ovarian cancer metastasis•SIK2 promotes ovarian cancer cell fatty acid oxidation through ACC phosphorylation•SIK2 activates the PI3K pathway through phosphorylation of p85α at S154 and S541 Miranda et al. show that in serous ovarian cancer SIK2 is overexpressed in adipocyte-rich metastatic deposits compared with primary lesions. Adipocytes induce calcium-dependent activation and autophosphorylation of SIK2, which drives tumor cell survival and metabolism. SIK2 depletion prevents metastasis in vivo.
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Vir: Osebne bibliografije
in: SICRIS
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