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J. Biol. Chem., Vol. 269, Issue 28, 18307-18310, Jul, 1994
YP Chen, TE O'Toole, T Shipley, J Forsyth, SE LaFlamme, KM Yamada, SJ Shattil and MH Ginsberg
The affinities of integrin alpha beta heterodimers for extracellular
ligands are important regulators of cell adhesion. Intracellular signals
provoke changes in the integrin extracellular domain resulting in
"activation," as manifested by an increase in affinity. Interactions of
integrin cytoplasmic domains with intracellular elements may mediate this
"inside-out signaling." Here we report that overexpression of chimeras of
the cytoplasmic domain of integrin beta 3 or beta 1 subunits, joined to the
extracellular and transmembrane domains of the Tac subunit of the
interleukin-2 receptor, reduced integrin affinity. In contrast, chimeras
containing the cytoplasmic domain of alpha 5 or alpha IIb or of beta 3
bearing a mutation that disrupts inside-out signaling lacked inhibitory
activity. These data suggest that limiting quantities of intracellular
factors bind to integrin beta 3 and beta 1 cytoplasmic domains to modulate
ligand binding affinity. Structural mimics of these domains may provide a
novel means to alter cell adhesion.
"Inside-out" signal transduction inhibited by isolated integrin cytoplasmic domains
Department of Vascular Biology, Scripps Research Institute, La Jolla, California 92037.
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