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PI3K/mTOR mediate mitogen-dependent HDAC1 phosphorylation in breast cancer:a novel regulation of estrogen receptor expression

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分子细胞生物学报:英文版 2015年第2期7卷 132-142页

作者： Simona Citro Claudia Miccolo Laura Meloni susanna chiocca Department of Experimental Oncology European Institute of OncologyIFOM-IEO Campusvia Adamello 1620139 MilanItaly Department for Molecular Biomedical Research Technologiepark Zwijnaarde927 VIB west9052 GhentBelgium

Histone deacetylase 1(HDAC1)is an important epigenetic controller involvedin transcriptional regulation throughmodification of chromatin *** and epigenetic changes and deregulation of signal transduction pathways have been implicated in the development of breast *** of estrogen receptor a(ERa)expression is one of the mechanisms behind the acquisition of endocrine *** and increased hormone and growth factor receptor signaling in breast cancer cells contribute to resistance to endocrine *** HDACs and the PI3K/mTOR signaling pathway are becoming promising targets in breast cancer,reversing also acquired hormone *** we show how mitogens,activating the PI3K/mTOR pathway,trigger the phosphorylation of HDAC1 in breast cancer cells,which is completely dependent on the activity of the p70 S6 kinase(S6K1).Our findings show that S6K1,overexpressed in many breast cancers,controls HDAC1-dependent transcriptional regulation of ERa levels upon mitogenic stimuli,controlling HDAC1 recruitment to the ERa ***,cell treatment with both mTOR and HDACs inhibitors shows an additive effect in inhibiting breast cancer *** confirms the novel cross-talk between the HDAC1 and PI3K pathways with clinical implications towards the treatment of this malignant disease.

关键词： breast cancer estrogen receptor HDAC1/mTOR/PI3K/S6K1

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SUMOylation regulates p27^(Kip1) stability and localization in response to TGFβ

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分子细胞生物学报:英文版 2016年第1期8卷 17-30页

作者： Sara Lovisa Simona Citro Maura Sonego Alessandra Dall’Acqua Valentina Ranzuglia Stefania Berton Alfonso Colombatti Barbara Belletti susanna chiocca Monica Schiappacassi Gustavo Baldassarre Division of Experimental Oncology 2 Centro di Riferimento Oncologico National Cancer InstituteAviano 33081Italy Department of Experimental Oncology European Institute of Oncology at the IFOM-IEO CampusMilan 20139Italy Department of Scienze e Tecnologie Biomediche MATI Center of ExcellenceUniversity of UdineUdine 33010Italy Present address:Department of Cancer Biology Metastasis Research CenterThe University of Texas MD Anderson Cancer CenterHoustonTX 77030USA.

Exposure of normal and tumor-derived cells to TGFbresults in different outcomes,depending on the regulation of key *** CDK inhibitor p27^(Kip1) is one of these TGFβ targets and is essential for the TGFβ-induced cell cycle *** treatment inhibits p27^(Kip1) degradation and induces its nuclear translocation,through mechanisms that are still *** evidences suggest that SUMOylation,a post-translational modification able to modulate the stability and subcellular localization of target proteins,critically modifies members of the TGFβ signaling ***,we demonstrate that p27^(Kip1) is SUMOylated in response to TGFβ *** different p27^(Kip1) point mutants,we identified lysine 134(K134)as the residue modified by small ubiquitin-like modifier 1(SUMO1)in response to TGFb ***β-induced K134 SUMOylation increased protein stability and nuclear localization of both endogenous and exogenously expressed p27^(Kip1).We observed thatSUMOylation regulated p27^(Kip1) binding to CDK2,thereby governing its nuclear proteasomal degradation through the phosphorylation of threonine ***,p27^(Kip1) SUMOylation was necessary for proper cell cycle exit following *** data indicate thatSUMOylation is a novel regulatory mechanism that modulates p27^(Kip1) function in response to TGFβ *** the involvement of TGFb signaling in cancer cell proliferation and invasion,our data may shed light on an important aspect of this pathway during tumor progression.

关键词： p^(27kip1) SUMOylation TGFβ

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Viral manipulation of cellular protein conjugation pathways: The SUMO lesson

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World Journal of Virology 2013年第2期2卷 79-90页

作者： Domenico Mattoscio Chiara V Segré susanna chiocca Department of Experimental Oncology European Institute of Oncology Via Adamello 16 20139 Milan Italy

Small ubiquitin-like modifier(SUMO)ylation is a key posttranslational modification mechanism that controls the function of a plethora of proteins and biological processes. Given its central regulatory role, it is not surprising that it is widely exploited by viruses. A number of viral proteins are known to modify and/or be modified by the SUMOylation system to exert their function, to create a cellular environment more favorable for virus survival and propagation, and to prevent host antiviral responses. Since the SUMO pathway is a multi-step cascade, viral proteins engage with it at many levels, to advance and favor each stage of a typical infection cycle: replication, viral assembly and immune evasion. Here we review the current knowledge on the interplay between the host SUMO system and viral lifecycle.

关键词： Virus Small ubiquitin-like modifier Small ubiquitin-like modifier-ylation Exploitation Virus assembly Immune evasion Innate immunity

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