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  • Cell Research
    200433 China 2 National Key Laboratory of Medical Immunology Institute of Immunology Second Military Medical University Shanghai 200433 China Correspondence Xuetao Cao Tel 86 21 5562 0605 Fax 86 21 6538 2502 E mail caoxt immunol org Yan Bao Tel 86 21 8187 1910 Fax 86 21 8187 1909 E mail baoy smmu 163 com Although B cells play important roles in the humoral immune response and the regulation of adaptive immunity B cell subpopulations with unique phenotypes particularly those with non classical immune functions should be further investigated By challenging mice with Listeria monocytogenes Escherichia coli vesicular stomatitis virus and Toll like receptor ligands we identified an inducible CD11ahiFcγRIIIhi B cell subpopulation that is significantly expanded and produces high levels of IFN γ during the early stage of the immune response This subpopulation of B cells can promote macrophage activation via generating IFN γ thereby facilitating the innate immune response against intracellular bacterial infection As this new subpopulation is of B cell origin and exhibits the phenotypic characteristics of B cells we designated these cells as IFN γ producing innate B cells Dendritic cells were essential for the inducible generation of these innate B cells from the follicular B

    Original URL path: http://www.cell-research.com/arts.asp?id=1881 (2016-02-14)
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  • Cell Research
    Xiao Fan Zhu 6 Tao Cheng 6 Yong Liang Zhao 1 Xinquan Wang 4 Jannie M Rendtlew Danielsen 1 7 Feng Liu 2 and Yun Gui Yang 1 8 1 Center For Genome Variations and Precision Bio Medicine Beijing Institute of Genomics Chinese Academy of Sciences Beijing 100101 China 2 State Key Laboratory of Biomembrane and Membrane Biotechnology Institute of Zoology Chinese Academy of Sciences Beijing 100101 China 3 Chinese Academy of Sciences Key Laboratory of Genome Sciences and Information Beijing Institute of Genomics Chinese Academy of Sciences Beijing 100101 China 4 Center for Structural Biology Ministry of Education Key Laboratory of Protein Sciences School of Life Sciences Tsinghua University Beijing 100084 China 5 Life Sciences Institute Zhejiang University Zhejiang 310058 China 6 State Key Laboratory of Experimental Hematology Institute of Hematology Tianjin 300041 China 7 The Novo Nordisk Foundation Center for Protein Research Ubiquitin Signalling Group Faculty of Health Sciences Copenhagen Denmark 8 University of Chinese Academy of Sciences 19A Yuquan Road Beijing 100049 China Correspondence Yun Gui Yang E mail ygyang big ac cn Feng Liu E mail liuf ioz ac cn The methyltransferase like 3 METTL3 containing methyltransferase complex catalyzes the N6 methyladenosine m6A formation a novel epitranscriptomic marker however the nature of this complex remains largely unknown Here we report two new components of the human m6A methyltransferase complex Wilms tumor 1 associating protein WTAP and methyltransferase like 14 METTL14 WTAP interacts with METTL3 and METTL14 and is required for their localization into nuclear speckles enriched with pre mRNA processing factors and for catalytic activity of the m6A methyltransferase in vivo The majority of RNAs bound by WTAP and METTL3 in vivo represent mRNAs containing the consensus m6A motif In the absence of WTAP the RNA binding capability of METTL3 is strongly reduced suggesting that WTAP

    Original URL path: http://www.cell-research.com/arts.asp?id=1882 (2016-02-14)
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  • Cell Research
    Stanevich 1 Nathan Wlodarchak 1 Rituparna Sengupta 1 Li Jiang 1 Kenneth A Satyshur 1 and Yongna Xing 1 1 McArdle Laboratory Department of Oncology University of Wisconsin at Madison School of Medicine and Public Health Madison WI 53706 USA Correspondence Yongna Xing E mail xing oncology wisc edu Proper activation of protein phosphatase 2A PP2A catalytic subunit is central for the complex PP2A regulation and is crucial for broad aspects of cellular function The crystal structure of PP2A bound to PP2A phosphatase activator PTPA and ATPγS reveals that PTPA makes broad contacts with the structural elements surrounding the PP2A active site and the adenine moiety of ATP PTPA binding stabilizes the protein fold of apo PP2A required for activation and orients ATP phosphoryl groups to bind directly to the PP2A active site This allows ATP to modulate the metal binding preferences of the PP2A active site and utilize the PP2A active site for ATP hydrolysis In vitro ATP selectively and drastically enhances binding of endogenous catalytic metal ions which requires ATP hydrolysis and is crucial for acquisition of pSer Thr specific phosphatase activity Furthermore both PP2A and ATP binding are required for PTPA function in cell proliferation and survival

    Original URL path: http://www.cell-research.com/arts.asp?id=1883 (2016-02-14)
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  • Cell Research
    1 Jie Ding 1 Fangyu Zhao 1 Chao Ge 1 Qifeng Wang 3 Taoyang Chen 4 Ming Yao 1 Jinjun Li 1 Jianren Gu1 and Xianghuo He 1 1 State Key Laboratory of Oncogenes and Related Genes Shanghai Cancer Institute Renji Hospital Shanghai Jiao Tong University School of Medicine Shanghai 200032 China 2 Shanghai Medical College Fudan University Shanghai 200032 China 3 Department of Pathology Fudan University Shanghai Cancer Center Shanghai Medical College Fudan University Shanghai 200032 China 4 Qidong Liver Cancer Institute Qidong Jiangsu 226200 China Correspondence Xianghuo He Tel Fax 86 21 64436539 E mail xhhe shsci org We have previously identified 1 241 regions of somatic copy number alterations CNAs in hepatocellular carcinoma HCC In the present study we found that a novel recurrent focal amplicon 1q24 1 24 2 targets the MPZL1 gene in HCC Notably there is a positive correlation between the expression levels of MPZL1 and intrahepatic metastasis of the HCC specimens MPZL1 can significantly enhance the migratory and metastatic potential of the HCC cells Moreover we found that one of the mechanisms by which MPZL1 promotes HCC cell migration is by inducing the phosphorylation and activation of the pro metastatic protein cortactin Additionally

    Original URL path: http://www.cell-research.com/arts.asp?id=1884 (2016-02-14)
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  • Cell Research
    USA Correspondence Ding Xue Tel 1 303 492 0271 E mail Ding Xue Colorado EDU During C elegans apoptosis the dicer ribonuclease DCR 1 is cleaved by the cell death protease CED 3 to generate a truncated DCR 1 tDCR 1 with one and a half ribonuclease III RNase III domains converting it into a deoxyribonuclease DNase that initiates apoptotic chromosome fragmentation We performed biochemical and functional analyses to understand this unexpected RNase to DNase conversion In full length DCR 1 tDCR 1 DNase activity is suppressed by its N terminal DCR 1 sequence However not all the sequence elements in the N terminal DCR 1 are required for this suppression Our deletion analysis reveals that a 20 residue α helix sequence in DCR 1 appears to define a critical break point for the sequence required for suppressing tDCR 1 DNase activity through a structure dependent mechanism Removal of the N terminal DCR 1 sequence from tDCR 1 activates a DNA binding activity that also requires the one half RNase IIIa domain and enables tDCR 1 to process DNA Consistently structural modeling of DCR 1 and tDCR 1 suggests that cleavage of DCR 1 by CED 3 may cause a

    Original URL path: http://www.cell-research.com/arts.asp?id=1885 (2016-02-14)
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  • Cell Research
    Biopolis Drive Singapore 138673 2 Department of Biochemistry and Howard Hughes Medical Institute University of Colorado Boulder Boulder CO 80303 USA 3 European Molecular Biology Laboratory 6 rue Jules Horowitz BP 181 38042 Grenoble France 4 Unit of Virus Host Cell Interactions UJF EMBL CNRS UMI 3265 6 rue Jules Horowitz 38042 Grenoble Cedex 9 France 5 Life Sciences Institute Zhejiang University 388 Yuhangtang Road Hangzhou Zhejiang 310000 China 6 Department of Biochemistry National University of Singapore 14 Science Drive Singapore 117543 Correspondence Haiwei Song Tel 65 65869700 E mail haiwei imcb a star edu sg The evolutionarily conserved Lsm1 7 Pat1 complex is the most critical activator of mRNA decapping in eukaryotic cells and plays many roles in normal decay AU rich element mediated decay and miRNA silencing yet how Pat1 interacts with the Lsm1 7 complex is unknown Here we show that Lsm2 and Lsm3 bridge the interaction between the C terminus of Pat1 Pat1C and the Lsm1 7 complex The Lsm2 3 Pat1C complex and the Lsm1 7 Pat1C complex stimulate decapping in vitro to a similar extent and exhibit similar RNA binding preference The crystal structure of the Lsm2 3 Pat1C complex shows that Pat1C binds

    Original URL path: http://www.cell-research.com/arts.asp?id=1886 (2016-02-14)
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  • Cell Research
    Sciences Tsinghua University Beijing 100084 China 2 Department of Molecular Cellular and Developmental Biology University of Colorado Boulder Colorado 80309 USA Correspondence Ding Xue E mail ding xue colorado edu Technologies to achieve specific and precise genome editing such as knock in and knock out are critical for deciphering the functions of a gene and for understanding fundamental biological processes Compared with the zinc finger nucleases ZFN and transcription activator

    Original URL path: http://www.cell-research.com/arts.asp?id=1887 (2016-02-14)
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  • Cell Research
    C elegans embryos requires cell death genes and is dispensable for development Guangshuo Ou 1 2 Christian Gentili 3 and Pierre Gönczy 3 1 National Laboratory of Biomacromolecules Institute of Biophysics Chinese Academy of Sciences 15 Datun Road Chaoyang District Beijing 100101 China 2 Tsinghua Peking Center for Life Sciences School of Life Sciences Tsinghua University Beijing 100101 China 3 Swiss Institute for Experimental Cancer Research ISREC School of Life Sciences Swiss Federal Institute of Technology Lausanne EPFL Lausanne CH 1015 Switzerland Correspondence Pierre Gönczy Email Pierre Gonczy epfl ch Guangshuo Ou E mail guangshuo ou gmail com The midbody is a structure formed within the intercellular bridge towards the end of cytokinesis1 Microtubules within this bridge are then severed on one side of the midbody during abscission thus generating a midbody remnant in one of the resulting daughter cells Midbody remnants persist long after cell division and accumulate preferentially in stem cells induced pluripotent stem iPS cells and cancer stem cells2 3 4 Upon induction of differentiation midbody remnants are degraded by autophagy or released into the extracellular milieu in some tissue culture cells and it has been proposed that such removal is critical for enabling a differentiation program2

    Original URL path: http://www.cell-research.com/arts.asp?id=1888 (2016-02-14)
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