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Clustered syk Tyrosine Kinase Domains Trigger Phagocytosis
Steven Greenberg, Peter Chang, Da-Cheng Wang, Ramnik Xavier and Brian Seed
Proceedings of the National Academy of Sciences of the United States of America
Vol. 93, No. 3 (Feb. 6, 1996), pp. 1103-1107
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/38755
Page Count: 5
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Phagocytosis is a phylogenetically primitive mechanism adapted by specialized cells of the immune system to ingest particulate pathogens. Recent evidence suggests that the program of specific cytoskeletal rearrangements that underlies phagocytosis may share elements with the antigen receptor signaling pathway in lymphocytes. Tyrosine phosphorylation, necessary for both lymphocyte effector function and phagocytosis, is thought to allow cytoskeletal elements to couple to the intracellular domains of antigen and Fc receptor subunits. We show here that the intracellular domains of the receptors are not inherently required for cytoskeletal coupling. Chimeric transmembrane proteins bearing syk but not src family tyrosine kinase domains are capable of autonomously triggering phagocytosis and redistribution of filamentous actin in COS cells. These responses cannot be initiated by a receptor chimera bearing a point mutation in the syk catalytic domain, and the kinase domain alone is sufficient for initiating cytoskeletal coupling.
Proceedings of the National Academy of Sciences of the United States of America © 1996 National Academy of Sciences