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Blood, Vol. 95 No. 9 (May 1), 2000:
pp. 2943-2946
Wiskott-Aldrich syndrome protein is necessary for efficient
IgG-mediated phagocytosis
Roberto Lorenzi,
Paul M. Brickell,
David R. Katz,
Christine Kinnon, and
Adrian J. Thrasher
Department of Molecular Immunology and Department of Molecular
Haematology, Institute of Child Health, London, England; Department of
Immunology, University College London Medical School, London, England.
Interactions between the Wiskott-Aldrich (WAS) protein (WASp), small
GTPases, and the cytoskeletal organizing complex Arp2/3 appear to be
critical for the transduction of signals from the cell membrane to the
actin cytoskeleton in hematopoietic cells. This study shows that
Fc -receptor (FcR)-mediated phagocytosis is impaired in
WASp-deficient peripheral blood monocytes, and that in macrophages,
formation of the actin cup and local recruitment of tyrosine
phosphorylated proteins is markedly attenuated. Results also show that,
in normal macrophages, WASp itself is actively recruited to the cup,
suggesting that assembly of this specialized cytoskeletal structure is
dependent on its expression.
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