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Del Pozo, M.A. et al.

Del Pozo, Kiosses, Alderson, Meller, Hahn, Schwartz,

Integrins regulate GTP-Rac localized effector interactions through dissociation of Rho-GDI.

The proper function of Rho GTPases requires precise spatial and temporal regulation of effector interactions. Integrin-mediated cell adhesion modulates the interaction of GTP-Rac with its effectors by controlling GTP-Rac membrane targeting. Here, we show that the translocation of GTP-Rac to membranes is independent of effector interactions, but instead requires the polybasic sequence near the carboxyl terminus. Cdc42 also requires integrin-mediated adhesion for translocation to membranes. A recently developed fluorescence resonance energy transfer (FRET)-based assay yields the surprising result that, despite its uniform distribution, the interaction of activated V12-Rac with a soluble, cytoplasmic effector domain is enhanced at specific regions near cell edges and is induced locally by integrin stimulation. This enhancement requires Rac membrane targeting. We show that Rho-GDI, which associates with cytoplasmic GTP-Rac, blocks effector binding. Release of Rho-GDI after membrane translocation allows Rac to bind to effectors. Thus, Rho-GDI confers spatially restricted regulation of Rac-effector interactions.[1]

References

Integrins regulate GTP-Rac localized effector interactions through dissociation of Rho-GDI. Del Pozo, M.A., Kiosses, W.B., Alderson, N.B., Meller, N., Hahn, K.M., Schwartz, M.A. Nat. Cell Biol. (2002) [Pubmed]

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