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    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
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