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| 1 | Viral manipulation of cellular protein conjugation pathways: The SUMO lesson显示文摘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. | Domenico Mattoscio Chiara V Segré Susanna Chiocca | 2013 | World Journal of Virology2013，2，2： | 8 |
| 2 | PI3K/mTOR mediate mitogen-dependent HDAC1 phosphorylation in breast cancer:a novel regulation of estrogen receptor expression显示文摘Histone deacetylase 1(HDAC1)is an important epigenetic controller involvedin transcriptional regulation throughmodification of chromatin structure.Genetic and epigenetic changes and deregulation of signal transduction pathways have been implicated in the development of breast cancer.Downregulation of estrogen receptor a(ERa)expression is one of the mechanisms behind the acquisition of endocrine resistance.Sustained and increased hormone and growth factor receptor signaling in breast cancer cells contribute to resistance to endocrine therapy.Both HDACs and the PI3K/mTOR signaling pathway are becoming promising targets in breast cancer,reversing also acquired hormone resistance.Here 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 promoter.Furthermore,cell treatment with both mTOR and HDACs inhibitors shows an additive effect in inhibiting breast cancer proliferation.This confirms the novel cross-talk between the HDAC1 and PI3K pathways with clinical implications towards the treatment of this malignant disease. | Simona Citro Claudia Miccolo Laura Meloni Susanna Chiocca | 2015 | Journal of Molecular Cell Biology2015，7，2： | 1 |
| 3 | Regulating the Regulators: The Post-Translational Code of Class I HDAC1 and HDAC2显示文摘 | Chiara V. Segré Susanna Chiocca Minoru Yoshida | 2010 | Journal of Biomedicine and Biotechnology2010，，： | 1 |
| 4 | Listeria monocytogenes: a bacterial pathogen to hit on the SUMO pathway显示文摘 | Simona Citro Susanna Chiocca | 2010 | Cell Research2010，20，7： | 0 |
| 5 | SUMOylation regulates p27^(Kip1) stability and localization in response to TGFβ显示文摘Exposure of normal and tumor-derived cells to TGFbresults in different outcomes,depending on the regulation of key targets.The CDK inhibitor p27^(Kip1) is one of these TGFβ targets and is essential for the TGFβ-induced cell cycle arrest.TGFb treatment inhibits p27^(Kip1) degradation and induces its nuclear translocation,through mechanisms that are still unknown.Recent 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 pathway.Here,we demonstrate that p27^(Kip1) is SUMOylated in response to TGFβ treatment.Using 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 treatment.TGFβ-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 187.Importantly,p27^(Kip1) SUMOylation was necessary for proper cell cycle exit following TGFbtreatment.These data indicate thatSUMOylation is a novel regulatory mechanism that modulates p27^(Kip1) function in response to TGFβ stimulation.Given 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. | Sara Lovisa Simona Citro Maura Sonego Alessandra Dall’Acqua Valentina Ranzuglia Stefania Berton Alfonso Colombatti Barbara Belletti Susanna Chiocca Monica Schiappacassi Gustavo Baldassarre | 2016 | Journal of Molecular Cell Biology2016，8，1： | 0 |
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