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J Biol Chem, Vol. 273, Issue 51, 33897-33900, December 18, 1998
From the Department of Vascular Biology, The Scripps Research
Institute, La Jolla, California 92037
Increased integrin ligand binding affinity
(activation) is triggered by intracellular signaling events. A
Ras-initiated mitogen-activated protein kinase pathway suppresses
integrin activation in fibroblasts. We used expression cloning to
isolate cDNAs that prevent Ras suppression of integrin activation.
Here, we report that PEA-15, a small death effector
domain (DED)-containing protein, blocks Ras
suppression. PEA-15 does not block the capacity of Ras to activate the
ERK mitogen-activated protein kinase pathway. Instead, it inhibits suppression via a pathway blocked by a dominant-negative form of the
distinct small GTPase, R-Ras. Heretofore, all known DEDs functioned in
the regulation of apoptosis. In contrast, the DED of PEA-15 is
essential for its capacity to reverse suppression of integrin
activation. Thus, certain DED-containing proteins can regulate integrin
activation as opposed to apoptotic protease cascades.
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