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J. Cell Biol.,
Volume 145, Number 4, May 17, 1999 889-897
v
3 Suppression of
Calcium/Calmodulin-dependent Protein Kinase II Regulates
51 Function
* Department of Anatomy and Cell Biology, State University of New York, Health Science Center at Syracuse, Syracuse, New
York 13210; Many cells express more than one integrin
receptor for extracellular matrix, and in vivo these receptors may be simultaneously engaged. Ligation of
one integrin may influence the behavior of others
on the cell, a phenomenon we have called integrin
crosstalk. Ligation of the integrin Department of Medicine, Infectious Diseases Division, Washington University School of Medicine, St. Louis,
Missouri, 63110; § Vascular Biology Unit, Laboratory of Cardiovascular Science, Gerontology Research Center, National
Institute on Aging, National Institutes of Health, Baltimore, Maryland 21224; and Program in Microbial Pathogenesis and Host
Defense, University of California, San Francisco, California 94143
v
3 inhibits both
phagocytosis and migration mediated by 51 on the
same cell, and the 3 cytoplasmic tail is necessary and
sufficient for this regulation of 51. Ligation of 51
activates the calcium- and calmodulin-dependent protein kinase II (CamKII). This activation is required
for 51-mediated phagocytosis and migration. Simultaneous ligation of v3 or expression of a chimeric
molecule with a free 3 cytoplasmic tail prevents 51-mediated activation of CamKII. Expression of a
constitutively active CamKII restores 51 functions
blocked by v3-initiated integrin crosstalk. Thus, v3
inhibition of 51 activation of CamKII is required for
its role in integrin crosstalk. Structure-function analysis
of the 3 cytoplasmic tail demonstrates a requirement for Ser752 in 3-mediated suppression of CamKII activation, while crosstalk is independent of Tyr747 and
Tyr759, implicating Ser752, but not 3 tyrosine phosphorylation in initiation of the v3 signal for integrin crosstalk.
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