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  1. Article ; Online: The Human Protein PRR14 Tethers Heterochromatin to the Nuclear Lamina during Interphase and Mitotic Exit

    Andrey Poleshko / Katelyn M. Mansfield / Caroline C. Burlingame / Mark D. Andrake / Neil R. Shah / Richard A. Katz

    Cell Reports, Vol 5, Iss 2, Pp 292-

    2013  Volume 301

    Abstract: The nuclear lamina is a protein meshwork that lies under the inner nuclear membrane of metazoan cells. One function of the nuclear lamina is to organize heterochromatin at the inner nuclear periphery. However, very little is known about how ... ...

    Abstract The nuclear lamina is a protein meshwork that lies under the inner nuclear membrane of metazoan cells. One function of the nuclear lamina is to organize heterochromatin at the inner nuclear periphery. However, very little is known about how heterochromatin attaches to the nuclear lamina and how such attachments are restored at mitotic exit. Here, we show that a previously unstudied human protein, PRR14, functions to tether heterochromatin to the nuclear periphery during interphase, through associations with heterochromatin protein 1 (HP1) and the nuclear lamina. During early mitosis, PRR14 is released from the nuclear lamina and chromatin and remains soluble. Strikingly, at the onset of anaphase, PRR14 is incorporated rapidly into chromatin through HP1 binding. Finally, in telophase, PRR14 relocalizes to the reforming nuclear lamina. This stepwise reassembly of PRR14 suggests a function in the selection of HP1-bound heterochromatin for reattachment to the nuclear lamina as cells exit mitosis.
    Keywords Biology (General) ; QH301-705.5
    Subject code 571
    Language English
    Publishing date 2013-10-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Transcription factor NF-κB is modulated by symbiotic status in a sea anemone model of cnidarian bleaching

    Katelyn M. Mansfield / Nicole M. Carter / Linda Nguyen / Phillip A. Cleves / Anar Alshanbayeva / Leah M. Williams / Camerron Crowder / Ashley R. Penvose / John R. Finnerty / Virginia M. Weis / Trevor W. Siggers / Thomas D. Gilmore

    Scientific Reports, Vol 7, Iss 1, Pp 1-

    2017  Volume 14

    Abstract: Abstract Transcription factor NF-κB plays a central role in immunity from fruit flies to humans, and NF-κB activity is altered in many human diseases. To investigate a role for NF-κB in immunity and disease on a broader evolutionary scale we have ... ...

    Abstract Abstract Transcription factor NF-κB plays a central role in immunity from fruit flies to humans, and NF-κB activity is altered in many human diseases. To investigate a role for NF-κB in immunity and disease on a broader evolutionary scale we have characterized NF-κB in a sea anemone (Exaiptasia pallida; called Aiptasia herein) model for cnidarian symbiosis and dysbiosis (i.e., “bleaching”). We show that the DNA-binding site specificity of Aiptasia NF-κB is similar to NF-κB proteins from a broad expanse of organisms. Analyses of NF-κB and IκB kinase proteins from Aiptasia suggest that non-canonical NF-κB processing is an evolutionarily ancient pathway, which can be reconstituted in human cells. In Aiptasia, NF-κB protein levels, DNA-binding activity, and tissue expression increase when loss of the algal symbiont Symbiodinium is induced by heat or chemical treatment. Kinetic analysis of NF-κB levels following loss of symbiosis show that NF-κB levels increase only after Symbiodinium is cleared. Moreover, introduction of Symbiodinium into naïve Aiptasia larvae results in a decrease in NF-κB expression. Our results suggest that Symbiodinium suppresses NF-κB in order to enable establishment of symbiosis in Aiptasia. These results are the first to demonstrate a link between changes in the conserved immune regulatory protein NF-κB and cnidarian symbiotic status.
    Keywords Medicine ; R ; Science ; Q
    Subject code 570
    Language English
    Publishing date 2017-11-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article: A conserved Toll-like receptor-to-NF-κB signaling pathway in the endangered coral Orbicella faveolata

    Williams, Leah M / Aarthia Chezian / Alex Schiffer / Amber Thiel / Brian Nguyen / Cecilia Chacko / David Mueller / Deena Qadir / Donovan Dowers / Emma Ryan / Erick Salas-Rodriguez / Felicia Estrada / Jake Awtry / Jiawen Kang / John Malinowski / Jorge H. Pinzón C / Joseph J. Brennan / Julianne Welsh / Katelyn M. Mansfield /
    Kathryn E. Spilios / Khusbu Patel / Laura D. Mydlarz / Lauren E. Fuess / Michelle Nguyen / Ndidi Njoku / Phuong Nguyen / Sarah A. Yunes / Sarah Banic / Sean Matuszak / Sinead Nguyen / Tessa Pliakas / Thomas D. Gilmore / Thomas McTigue / Wanwen Li / William Pellegrini / Yu-Hsuan Hsieh / Zoe Malchiodi

    Developmental and comparative immunology. 2018 Feb., v. 79

    2018  

    Abstract: Herein, we characterize the Toll-like receptor (TLR)-to-NF-κB innate immune pathway of Orbicella faveolata (Of), which is an ecologically important, disease-susceptible, reef-building coral. As compared to human TLRs, the intracellular TIR domain of Of- ... ...

    Abstract Herein, we characterize the Toll-like receptor (TLR)-to-NF-κB innate immune pathway of Orbicella faveolata (Of), which is an ecologically important, disease-susceptible, reef-building coral. As compared to human TLRs, the intracellular TIR domain of Of-TLR is most similar to TLR4, and it can interact in vitro with the human TLR4 adapter MYD88. Treatment of O. faveolata tissue with lipopolysaccharide, a ligand for mammalian TLR4, resulted in gene expression changes consistent with NF-κB pathway mobilization. Biochemical and cell-based assays revealed that Of-NF-κB resembles the mammalian non-canonical NF-κB protein p100 in that C-terminal truncation results in translocation of Of-NF-κB to the nucleus and increases its DNA-binding and transcriptional activation activities. Moreover, human IκB kinase (IKK) and Of-IKK can both phosphorylate conserved residues in Of-NF-κB in vitro and induce C-terminal processing of Of-NF-κB in vivo. These results are the first characterization of TLR-to-NF-κB signaling proteins in an endangered coral, and suggest that these corals have conserved innate immune pathways.
    Keywords coral reefs ; corals ; humans ; IKappaB kinase ; ligands ; lipopolysaccharides ; signal transduction ; Toll-like receptor 4 ; transcription factor NF-kappa B ; transcriptional activation
    Language English
    Dates of publication 2018-02
    Size p. 128-136.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 752411-0
    ISSN 1879-0089 ; 0145-305X
    ISSN (online) 1879-0089
    ISSN 0145-305X
    DOI 10.1016/j.dci.2017.10.016
    Database NAL-Catalogue (AGRICOLA)

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