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J Biol Chem, Vol. 273, Issue 24, 14853-14861, June 12, 1998
2
Integrin Adhesion Pathway and Induces Membrane Recruitment of
Cytohesin-1
From the Laboratorium für Molekulare Biologie, Genzentrum der
Universität München, Feodor-Lynen-Strasse 25, 81377 München, Germany
Signal transduction through
phosphoinositide 3-OH kinase (PI 3-kinase) has been implicated in the
regulation of lymphocyte adhesion mediated by integrin receptors.
Cellular phosphorylation products of PI 3-kinases interact with a
subset of pleckstrin homology (PH) domains, a module that has been
shown to recruit proteins to cellular membranes. We have recently
identified cytohesin-1, a cytoplasmic regulator of
2 integrin adhesion to intercellular adhesion
molecule 1. We describe here that expression of a constitutively active
PI 3-kinase is sufficient for the activation of Jurkat cell adhesion to
intercellular adhesion molecule 1, and for enhanced membrane
association of cytohesin-1. Up-regulation of cell adhesion by PI
3-kinase and membrane association of endogenous cytohesin-1 is
abrogated by overexpression of the isolated cytohesin-1 PH domain, but
not by a mutant of the PH domain which fails to associate with the
plasma membrane. The PH domain of Bruton's tyrosine kinase (Btk),
although strongly associated with the plasma membrane, had no effect on
either membrane recruitment of cytohesin-1 or on induction of adhesion
by PI 3-kinase. Having delineated the critical steps of the
2 integrin activation pathway by biochemical and
functional analyses, we conclude that PI 3-kinase activates inside-out
signaling of 2 integrins at least partially through cytohesin-1.
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