alexa Integrins regulate Rac targeting by internalization of membrane domains.
Molecular Biology

Molecular Biology

Journal of Cell Science & Therapy

Author(s): del Pozo MA, Alderson NB, Kiosses WB, Chiang HH, Anderson RG,

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Abstract Translocation of the small GTP-binding protein Rac1 to the cell plasma membrane is essential for activating downstream effectors and requires integrin-mediated adhesion of cells to extracellular matrix. We report that active Rac1 binds preferentially to low-density, cholesterol-rich membranes, and specificity is determined at least in part by membrane lipids. Cell detachment triggered internalization of plasma membrane cholesterol and lipid raft markers. Preventing internalization maintained Rac1 membrane targeting and effector activation in nonadherent cells. Regulation of lipid rafts by integrin signals may regulate the location of membrane domains such as lipid rafts and thereby control domain-specific signaling events in anchorage-dependent cells. This article was published in Science and referenced in Journal of Cell Science & Therapy

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