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  • Cell Research
    Schajnovitz 1 2 3 and David T Scadden 1 2 3 1 Center for Regenerative Medicine Massachusetts General Hospital Boston MA 02114 USA 2 Department of Stem Cell and Regenerative Biology Harvard University Cambridge MA 02138 USA 3 Harvard Stem Cell Institute Cambridge MA 02138 USA Correspondence David T Scadden E mail david scadden harvard edu Bone lining osteolineage cells were previously implicated as contributors to hematological disorders and malignancies

    Original URL path: http://www.cell-research.com/arts.asp?id=1904 (2016-02-14)
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  • Cell Research
    3 1 Inserm Unit 1110 Université de Strasbourg 3 rue Koeberlé F 67000 Strasbourg France 2 Pôle Hépato digestif Université de Strasbourg Strasbourg France 3 Hôpitaux Universitaires de Strasbourg Strasbourg France Correspondence Thomas F Baumert Tel 33 3 68 85 37 03 Fax 33 3 68 85 37 50 E mail Thomas Baumert unistra fr The high variability and the limited knowledge of the structure of the hepatitis C virus

    Original URL path: http://www.cell-research.com/arts.asp?id=1905 (2016-02-14)
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  • Cell Research
    387 388 Mitofusins ubiquitylation promotes fusion FREE Mafalda Escobar Henriques 1 1 Institute for Genetics Centre for Molecular Medicine CMMC Cologne Excellence Cluster on Cellular Stress Responses in Aging Associated Diseases CECAD University of Cologne Zülpicher Str 47a 50674 Cologne Germany Correspondence Mafalda Escobar Henriques E mail Mafalda Escobar uni koeln de Mitochondrial genes including Mfn2 are at the center of many diseases underscoring their potential as a therapeutical target

    Original URL path: http://www.cell-research.com/arts.asp?id=1916 (2016-02-14)
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  • Cell Research
    Liang 3 Linchang Dai 3 Xiaojun Ding 2 She Chen 2 Zhuqiang Zhang 2 3 Bing Zhu 1 2 3 and Zheng Zhou 3 5 1 Graduate Program Peking Union Medical College and Chinese Academy of Medical Sciences Beijing 100730 China 2 National Institute of Biological Sciences Beijing 102206 China 3 National Laboratory of Biomacromolecules Institute of Biophysics Chinese Academy of Sciences Beijing 100101 China 4 College of Plant Science and Technology Beijing University of Agriculture Beijing 102206 China 5 Center for Age related Diseases Peking University Health Science Center Beijing 100191 China Correspondence Zheng Zhou E mail zhouzh sun5 ibp ac cn Bing Zhu E mail zhubing nibs ac cn Zhuqiang Zhang E mail zhangzhuqiang nibs ac cn H2A Z is a highly conserved histone variant in all species The chromatin deposition of H2A Z is specifically catalyzed by the yeast chromatin remodeling complex SWR1 and its mammalian counterpart SRCAP However the mechanism by which H2A Z is preferentially recognized by non histone proteins remains elusive Here we identified Anp32e a novel higher eukaryote specific histone chaperone for H2A Z Anp32e preferentially associates with H2A Z H2B dimers rather than H2A H2B dimers in vitro and in vivo and dissociates non nucleosomal aggregates formed by DNA and H2A H2B We determined the crystal structure of the Anp32e chaperone domain 186 232 in complex with the H2A Z H2B dimer In this structure the region containing Anp32e residues 214 224 which is absent in other Anp32 family proteins specifically interacts with the extended H2A Z αC helix which exhibits an unexpected conformational change Genome wide profiling of Anp32e revealed a remarkable co occupancy between Anp32e and H2A Z Cells overexpressing Anp32e displayed a strong global H2A Z loss at the 1 nucleosomes whereas cells depleted of Anp32e displayed a moderate

    Original URL path: http://www.cell-research.com/arts.asp?id=1906 (2016-02-14)
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  • Cell Research
    of Biocontrol College of Life Sciences Sun Yat sen University Guangzhou 510275 China 2 Center for Inflammation and Epigenetics The Methodist Hospital Research Institute Houston TX 77030 USA 3 Central Laboratory The First Affiliated Hospital Jilin University Changchun 130012 China 4 Institute of Biosciences and Technology Texas A M University Health Science Center Houston TX 77030 USA Correspondence Jun Cui E mail cuij5 mail sysu edu cn Rong Fu Wang E mail E mail rwang3 tmhs org Lysine 63 K63 linked ubiquitination of RIG I plays a critical role in the activation of type I interferon pathway yet the molecular mechanism responsible for its deubiquitination is still poorly understood Here we report that the deubiquitination enzyme ubiquitin specific protease 3 USP3 negatively regulates the activation of type I interferon signaling by targeting RIG I Knockdown of USP3 specifically enhanced K63 linked ubiquitination of RIG I upregulated the phosphorylation of IRF3 and augmented the production of type I interferon cytokines and antiviral immunity We further show that there is no interaction between USP3 and RIG I like receptors RLRs in unstimulated or uninfected cells but upon viral infection or ligand stimulation USP3 binds to the caspase activation recruitment domain of RLRs

    Original URL path: http://www.cell-research.com/arts.asp?id=1907 (2016-02-14)
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  • Cell Research
    Liang 1 Huabin Ma 1 Wenjuan Li 1 Zhenru Zhou 1 Jie Li 1 Yan Ding 1 Junming Ren 1 Juan Lin 1 Felicia Han 1 Jianfeng Wu 1 and Jiahuai Han 1 1 State Key Laboratory of Cellular Stress Biology Innovation Center for Cell Biology School of Life Sciences Xiamen University Xiamen China Correspondence Jiahuai Han E mail jhan xmu edu cn E mail jhan scripps edu Formation of multi component signaling complex necrosomes is essential for tumor necrosis factor α TNF induced programmed necrosis also called necroptosis However the mechanisms of necroptosis are still largely unknown We isolated a TNF resistant L929 mutant cell line generated by retrovirus insertion and identified that disruption of the guanine nucleotide binding protein γ 10 Gγ10 gene is responsible for this phenotype We further show that Gγ10 is involved in TNF induced necroptosis and Gβ2 is the partner of Gγ10 Src is the downstream effector of Gβ2γ10 in TNF induced necroptosis because TNF induced Src activation was impaired upon Gγ10 knockdown Gγ10 does not affect TNF induced activation of NF κB and MAPKs and the formation of necrosomes but is required for trafficking of necrosomes to their potential functioning site an unidentified

    Original URL path: http://www.cell-research.com/arts.asp?id=1908 (2016-02-14)
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  • Cell Research
    1 Johan Holmberg 3 4 Shaobo Jin 4 John E Eriksson 1 2 Urban Lendahl 4 and Cecilia Sahlgren 1 2 5 1 Turku Centre for Biotechnology University of Turku and Åbo Akademi University 20520 Turku Finland 2 Department of Biosciences Åbo Akademi University 20520 Turku Finland 3 Ludwig Institute for Cancer Research Karolinska Institute Box 240 SE 171 77 Stockholm Sweden 4 Department of Cell and Molecular Biology Karolinska Institutet SE 171 77 Stockholm Sweden 5Department of Biomedical Engineering Technical University of Eindhoven 2612 Eindhoven The Netherlands Correspondence Cecilia Sahlgren E mail cecilia sahlgren btk fi Activation of Notch signaling requires intracellular routing of the receptor but the mechanisms controlling the distinct steps in the routing process is poorly understood We identify PKCζ as a key regulator of Notch receptor intracellular routing When PKCζ was inhibited in the developing chick central nervous system and in cultured myoblasts Notch stimulated cells were allowed to undergo differentiation PKCζ phosphorylates membrane tethered forms of Notch and regulates two distinct routing steps depending on the Notch activation state When Notch is activated PKCζ promotes re localization of Notch from late endosomes to the nucleus and enhances production of the Notch intracellular domain which

    Original URL path: http://www.cell-research.com/arts.asp?id=1909 (2016-02-14)
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  • Cell Research
    Clear Water Bay Kowloon Hong Kong China 2 Center of Systems Biology and Human Health School of Science and Institute for Advanced Study Hong Kong University of Science and Technology Clear Water Bay Kowloon Hong Kong China 3 Department of Neurology Institute of Molecular Medicine and Genetics Medical College of Georgia Georgia Regents University Augusta GA 30912 USA 4 Current address The Gurdon Institute University of Cambridge Tennis Court Road Cambridge CB2 1QN UK Correspondence Mingjie Zhang E mail mzhang ust hk The tumor suppressors Discs Large Dlg Lethal giant larvae Lgl and Scribble are essential for the establishment and maintenance of epithelial cell polarity in metazoan Dlg Lgl and Scribble are known to interact strongly with each other genetically and form the evolutionarily conserved Scribble complex Despite more than a decade of extensive research it has not been demonstrated whether Dlg Lgl and Scribble physically interact with each other Here we show that Dlg directly interacts with Lgl in a phosphorylation dependent manner Phosphorylation of any one of the three conserved Ser residues situated in the central linker region of Lgl is sufficient for its binding to the Dlg guanylate kinase GK domain The crystal structures of the Dlg4

    Original URL path: http://www.cell-research.com/arts.asp?id=1910 (2016-02-14)
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