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Building the phagocytic cup on an actin scaffold
Institution:1. Department of Cell and Developmental Biology, State University of New York Upstate Medical University, Syracuse, NY, 13210, USA;2. IFOM, FIRC Institute of Molecular Oncology, Milan, 20139, Italy;1. Department of Systems Biology, Blavatnik Institute at Harvard Medical School, 210 Longwood Avenue, Boston, MA 02115, USA;2. Department of Radiation Oncology, Dana-Farber Brigham Cancer Center, 75 Francis St, Boston, MA 02115, USA;3. Ludwig Center at Harvard, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02215, USA;1. Faculty of Science, University of Amsterdam, Amsterdam, the Netherlands;2. Australian Regenerative Medicine Institute, Monash University, Clayton, Victoria, Australia;1. The Kennedy Institute of Rheumatology, The University of Oxford, Oxford OX3 7FY, UK;2. Radcliffe Department of Medicine and MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, The University of Oxford, Oxford OX3 9DS, UK
Abstract:Cells ingest large particles, such as bacteria, viruses, or apoptotic cells, via the process of phagocytosis, which involves formation of an actin-rich structure known as the phagocytic cup. Phagocytic cup assembly and closure results from a concerted action of phagocytic receptors, regulators of actin polymerization, and myosin motors. Recent studies using advanced imaging approaches and biophysical techniques have revealed new information regarding phagocytic cup architecture, regulation of actin assembly, and the distribution, direction, and magnitude of the forces produced by the cytoskeletal elements that form the cup. These findings provide insights into the mechanisms leading to the assembly, expansion, and closure of phagocytic cups. The new data show that engulfment and internalization of phagocytic targets rely on several distinct yet complementary mechanisms that support the robust uptake of foreign objects and may be precisely tailored to the demands of specific phagocytic pathways.
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