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Myosin II‐dependent exclusion of CD45 from the site of Fcγ receptor activation during phagocytosis
Author(s) -
Yamauchi Shota,
Kawauchi Keiko,
Sawada Yasuhiro
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.06.041
Subject(s) - myosin , syk , phagocytosis , phosphorylation , chemistry , protein tyrosine phosphatase , fc receptor , receptor , tyrosine , tyrosine phosphorylation , myosin light chain kinase , phosphatase , microbiology and biotechnology , immunoreceptor tyrosine based activation motif , biochemistry , biophysics , biology , tyrosine kinase
Fcγ receptor (FcγR)‐mediated phagocytosis requires myosin II activity. Here we show that myosin II contributes to FcγR activation and subsequent F‐actin assembly at the nascent phagocytic cup. Inhibition of myosin II attenuates phosphorylation of the immunoreceptor tyrosine‐based activation motif (ITAM) of FcγR and binding of Syk to the ITAM. Furthermore, FcγR clusters independently of myosin II activity at the phagocytic cup, from which the receptor‐like protein tyrosine phosphatase CD45 is excluded depending on myosin II activity. These findings suggest that myosin II‐dependent segregation of CD45 from FcγR facilitates phosphorylation of the ITAM and triggers phagocytosis.