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(Received for publication, March 5, 1996, and in revised form, April 22, 1996)
From the Department of Clustering of several multisubunit receptors on
hematopoetic cells results in a signaling cascade involving the
phosphorylation of immunoreceptor tyrosine activation motifs, or
``ITAMs,'' and actin polymerization. Recent experiments indicate that
direct clustering of the ITAM-binding protein, p72syk (Syk), is
capable of transmitting a phagocytic signal in COS cells (Greenberg,
S., Chang, P., Wang, D., Xavier, R., and Seed, B. (1996) Proc.
Natl. Acad. Sci. U. S. A. 93, 1103-1107). However, the
possibility of redundant signaling pathways makes it difficult to test
the requirement for Syk in ITAM-dependent actin
polymerization in hematopoetic cells. We developed a model system to
study ITAM-dependent actin assembly. DT40 lymphocytes were
transfected with fusion proteins encoding the transmembrane and
cytosolic domains of the ITAM-containing
Volume 271, Number 28,
Issue of July 12, 1996
pp. 16597-16602
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
Medicine, Pulmonary Division,
College of Physicians and Surgeons, Columbia University, New York,
New York 10032, the Department of § Cardiovascular Molecular
Biology, Lederle Laboratories, Pearl River, New York, New York
10965, and Section of Immunobiology, Yale University School of
Medicine, New Haven, Connecticut 06510
subunit of Fc receptors.
Clustering the -containing fusion proteins with IgG-coated
erythrocytes triggered submembranous actin assembly. This response
depended on an intact ITAM, was absent in cell lines that had been
engineered to lack Syk, and was augmented in cell lines that stably
overexpressed Syk. These experiments demonstrate an absolute
requirement for Syk tyrosine kinase in ITAM-dependent actin
assembly in transfected lymphocytes.
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