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  • 1
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    Physiological regulation of the immunological synapse by agrin (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-05-12
    Description: T cell activation is dependent on both a primary signal delivered through the T cell receptor and a secondary costimulatory signal mediated by coreceptors. Although controversial, costimulation is thought to act through the specific redistribution and clustering of membrane and intracellular kinase-rich lipid raft microdomains at the contact site between T cells and antigen-presenting cells. This site has been termed the immunological synapse. Endogenous mediators of raft clustering in lymphocytes have not been identified, although they are essential for T cell activation. We now demonstrate that agrin, an aggregating protein crucial for formation of the neuromuscular junction, is also expressed in lymphocytes and is important in reorganization of membrane lipid microdomains and setting the threshold for T cell signaling. Our data show that agrin induces the aggregation of signaling proteins and the creation of signaling domains in both immune and nervous systems through a common lipid raft pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khan, A A -- Bose, C -- Yam, L S -- Soloski, M J -- Rupp, F -- R01AI20922/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 1;292(5522):1681-6. Epub 2001 May 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Outer Banks Neuroscience, Baltimore, MD 21218, USA. outerbanksneuro@yahoo.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11349136" target="_blank"〉PubMed〈/a〉
    Keywords: Agrin/genetics/metabolism/*physiology ; Alternative Splicing ; Animals ; Antigen-Presenting Cells/immunology/*physiology ; B-Lymphocytes/metabolism ; Glycosylation ; *Lymphocyte Activation ; Male ; Membrane Microdomains/*physiology ; Mice ; Neuromuscular Junction/physiology ; Neurons/physiology ; Rats ; Rats, Sprague-Dawley ; Receptor Aggregation ; Receptors, Antigen, T-Cell/physiology ; Receptors, Cholinergic/physiology ; Signal Transduction ; T-Lymphocyte Subsets/metabolism ; T-Lymphocytes/immunology/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    IFNalpha activates dormant haematopoietic stem cells in vivo (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-02-13
    Description: Maintenance of the blood system is dependent on dormant haematopoietic stem cells (HSCs) with long-term self-renewal capacity. After injury these cells are induced to proliferate to quickly re-establish homeostasis. The signalling molecules promoting the exit of HSCs out of the dormant stage remain largely unknown. Here we show that in response to treatment of mice with interferon-alpha (IFNalpha), HSCs efficiently exit G(0) and enter an active cell cycle. HSCs respond to IFNalpha treatment by the increased phosphorylation of STAT1 and PKB/Akt (also known as AKT1), the expression of IFNalpha target genes, and the upregulation of stem cell antigen-1 (Sca-1, also known as LY6A). HSCs lacking the IFNalpha/beta receptor (IFNAR), STAT1 (ref. 3) or Sca-1 (ref. 4) are insensitive to IFNalpha stimulation, demonstrating that STAT1 and Sca-1 mediate IFNalpha-induced HSC proliferation. Although dormant HSCs are resistant to the anti-proliferative chemotherapeutic agent 5-fluoro-uracil, HSCs pre-treated (primed) with IFNalpha and thus induced to proliferate are efficiently eliminated by 5-fluoro-uracil exposure in vivo. Conversely, HSCs chronically activated by IFNalpha are functionally compromised and are rapidly out-competed by non-activatable Ifnar(-/-) cells in competitive repopulation assays. Whereas chronic activation of the IFNalpha pathway in HSCs impairs their function, acute IFNalpha treatment promotes the proliferation of dormant HSCs in vivo. These data may help to clarify the so far unexplained clinical effects of IFNalpha on leukaemic cells, and raise the possibility for new applications of type I interferons to target cancer stem cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Essers, Marieke A G -- Offner, Sandra -- Blanco-Bose, William E -- Waibler, Zoe -- Kalinke, Ulrich -- Duchosal, Michel A -- Trumpp, Andreas -- England -- Nature. 2009 Apr 16;458(7240):904-8. doi: 10.1038/nature07815. Epub 2009 Feb 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Stem Cells and Cancer, Deutsches Krebsforschungszentrum (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19212321" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Ly/metabolism ; Cell Count ; Cell Cycle/*drug effects ; Cell Proliferation/drug effects ; Fluorouracil/pharmacology ; Hematopoietic Stem Cells/*cytology/*drug effects ; Interferon-alpha/*pharmacology ; Membrane Proteins/deficiency/metabolism ; Mice ; Mice, Inbred C57BL ; Phosphorylation/drug effects ; Receptor, Interferon alpha-beta/deficiency/metabolism ; STAT1 Transcription Factor/deficiency/metabolism ; Signal Transduction/drug effects ; Up-Regulation/drug effects
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Rel-associated pp40: an inhibitor of the rel family of transcription factors (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-23
    Description: The Rel-associated protein pp40 is functionally related to I kappa B, an inhibitor of the transcription factor NF-kappa B. Purified pp40 inhibits the DNA binding activity of the NF-kappa B protein complex (p50:p65 heterodimers), p50:c-Rel heteromers, and c-Rel homodimers. The sequence of the complementary DNA encoding pp40 revealed similarity to the gene encoding MAD-3, a protein with mammalian I kappa B-like activity. Protein sequencing of I kappa B purified from rabbit lung confirmed that MAD-3 encodes a protein similar to I kappa B. The sequence similarity between MAD-3 and pp40 includes a casein kinase II and consensus tyrosine phosphorylation site, as well as five repeats of a sequence found in the human erythrocyte protein ankyrin. These results suggest that rel-related transcription factors, which are capable of cytosolic to nuclear translocation, may be held in the cytosol by interaction with related cytoplasmic anchor molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, N -- Ghosh, S -- Simmons, D L -- Tempst, P -- Liou, H C -- Baltimore, D -- Bose, H R Jr -- CA09583/CA/NCI NIH HHS/ -- CA2616/CA/NCI NIH HHS/ -- CA33192/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1268-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Texas, Austin 78712.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1891714" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; Chick Embryo ; Cloning, Molecular ; DNA Probes ; Molecular Sequence Data ; NF-kappa B/*antagonists & inhibitors ; Oligonucleotide Probes ; Oncogene Proteins v-rel ; Open Reading Frames ; Phosphoproteins/*genetics/metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors ; RNA, Messenger/genetics ; Retroviridae Proteins, Oncogenic/*antagonists & inhibitors ; Sequence Homology, Nucleic Acid ; Transcription Factors/*antagonists & inhibitors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    High-throughput mapping of a dynamic signaling network in mammalian cells (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-12
    Description: Signaling pathways transmit information through protein interaction networks that are dynamically regulated by complex extracellular cues. We developed LUMIER (for luminescence-based mammalian interactome mapping), an automated high-throughput technology, to map protein-protein interaction networks systematically in mammalian cells and applied it to the transforming growth factor-beta (TGFbeta) pathway. Analysis using self-organizing maps and k-means clustering identified links of the TGFbeta pathway to the p21-activated kinase (PAK) network, to the polarity complex, and to Occludin, a structural component of tight junctions. We show that Occludin regulates TGFbeta type I receptor localization for efficient TGFbeta-dependent dissolution of tight junctions during epithelial-to-mesenchymal transitions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barrios-Rodiles, Miriam -- Brown, Kevin R -- Ozdamar, Barish -- Bose, Rohit -- Liu, Zhong -- Donovan, Robert S -- Shinjo, Fukiko -- Liu, Yongmei -- Dembowy, Joanna -- Taylor, Ian W -- Luga, Valbona -- Przulj, Natasa -- Robinson, Mark -- Suzuki, Harukazu -- Hayashizaki, Yoshihide -- Jurisica, Igor -- Wrana, Jeffrey L -- P50 GM-62413/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1621-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada, M5G 1X5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15761153" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors, Type I/metabolism ; Animals ; Cell Line ; Cell Polarity ; DNA-Binding Proteins/metabolism ; Epithelial Cells/cytology/physiology ; Humans ; Immunoprecipitation ; Luciferases ; Membrane Proteins/metabolism ; Mesoderm/cytology ; Mice ; Occludin ; Phosphorylation ; *Protein Interaction Mapping ; Protein-Serine-Threonine Kinases/metabolism ; Receptors, Transforming Growth Factor beta/metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Smad2 Protein ; Smad4 Protein ; Tight Junctions/ultrastructure ; Trans-Activators/metabolism ; Transforming Growth Factor beta/*metabolism ; p21-Activated Kinases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-12
    Description: The transition of cells from an epithelial to a mesenchymal phenotype is a critical event during morphogenesis in multicellular organisms and underlies the pathology of many diseases, including the invasive phenotype associated with metastatic carcinomas. Transforming growth factor beta (TGFbeta) is a key regulator of epithelial-to-mesenchymal transition (EMT). However, the molecular mechanisms that control the dissolution of tight junctions, an early event in EMT, remain elusive. We demonstrate that Par6, a regulator of epithelial cell polarity and tight-junction assembly, interacts with TGFbeta receptors and is a substrate of the type II receptor, TbetaRII. Phosphorylation of Par6 is required for TGFbeta-dependent EMT in mammary gland epithelial cells and controls the interaction of Par6 with the E3 ubiquitin ligase Smurf1. Smurf1, in turn, targets the guanosine triphosphatase RhoA for degradation, thereby leading to a loss of tight junctions. These studies define how an extracellular cue signals to the polarity machinery to control epithelial cell morphology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ozdamar, Barish -- Bose, Rohit -- Barrios-Rodiles, Miriam -- Wang, Hong-Rui -- Zhang, Yue -- Wrana, Jeffrey L -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1603-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Genetics and Microbiology, University of Toronto, Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15761148" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors, Type I/*metabolism ; Amino Acid Sequence ; Animals ; Cell Line ; Cell Polarity ; DNA-Binding Proteins/metabolism ; Epithelial Cells/*cytology/*physiology ; Humans ; Mesoderm/cytology ; Mice ; Models, Biological ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Binding ; Protein Kinase C/metabolism ; Protein Kinase C-epsilon ; Protein-Serine-Threonine Kinases ; Proteins/genetics/*metabolism ; Receptors, Transforming Growth Factor beta/*metabolism ; Smad2 Protein ; Tight Junctions/metabolism/ultrastructure ; Trans-Activators/metabolism ; Transforming Growth Factor beta/metabolism/pharmacology ; Ubiquitin-Protein Ligases/metabolism ; rhoA GTP-Binding Protein/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Activation of the innate immune receptor Dectin-1 upon formation of a 'phagocytic synapse' (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-04-29
    Description: Innate immune cells must be able to distinguish between direct binding to microbes and detection of components shed from the surface of microbes located at a distance. Dectin-1 (also known as CLEC7A) is a pattern-recognition receptor expressed by myeloid phagocytes (macrophages, dendritic cells and neutrophils) that detects beta-glucans in fungal cell walls and triggers direct cellular antimicrobial activity, including phagocytosis and production of reactive oxygen species (ROS). In contrast to inflammatory responses stimulated upon detection of soluble ligands by other pattern-recognition receptors, such as Toll-like receptors (TLRs), these responses are only useful when a cell comes into direct contact with a microbe and must not be spuriously activated by soluble stimuli. In this study we show that, despite its ability to bind both soluble and particulate beta-glucan polymers, Dectin-1 signalling is only activated by particulate beta-glucans, which cluster the receptor in synapse-like structures from which regulatory tyrosine phosphatases CD45 and CD148 (also known as PTPRC and PTPRJ, respectively) are excluded (Supplementary Fig. 1). The 'phagocytic synapse' now provides a model mechanism by which innate immune receptors can distinguish direct microbial contact from detection of microbes at a distance, thereby initiating direct cellular antimicrobial responses only when they are required.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3084546/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3084546/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goodridge, Helen S -- Reyes, Christopher N -- Becker, Courtney A -- Katsumoto, Tamiko R -- Ma, Jun -- Wolf, Andrea J -- Bose, Nandita -- Chan, Anissa S H -- Magee, Andrew S -- Danielson, Michael E -- Weiss, Arthur -- Vasilakos, John P -- Underhill, David M -- AI066120/AI/NIAID NIH HHS/ -- AI071116/AI/NIAID NIH HHS/ -- R01 AI066120/AI/NIAID NIH HHS/ -- R01 AI066120-05/AI/NIAID NIH HHS/ -- R01 AI071116/AI/NIAID NIH HHS/ -- R01 AI071116-04/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2011 Apr 28;472(7344):471-5. doi: 10.1038/nature10071.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉IBD and Immunobiology Research Institute, 8700 Beverly Boulevard, Cedars-Sinai Medical Center, Los Angeles, California 90048, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21525931" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD45/deficiency/metabolism ; Cell Wall/chemistry/immunology ; Cells, Cultured ; Humans ; Immunity, Innate/*immunology ; Immunological Synapses/*immunology ; Lectins, C-Type ; Macrophages/immunology ; Membrane Proteins/deficiency/genetics/*immunology ; Mice ; *Models, Immunological ; Nerve Tissue Proteins/deficiency/genetics/*immunology ; Phagocytosis/*immunology ; Reactive Oxygen Species/metabolism ; Receptor-Like Protein Tyrosine Phosphatases, Class 3/deficiency/metabolism ; Saccharomyces cerevisiae/chemistry/immunology ; Signal Transduction/immunology ; Solubility ; beta-Glucans/chemistry/immunology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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