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  • New factor in cell migration

    images61The ability of locomotion of cells to certain stimuli requires deep and dynamic changes in cell morphology and cell adhesion. Many of these attractive stimuli in the cell membrane activate G protein-coupled receptor (GPCR), which emit signals that modify the one hand, the actin cytoskeleton, allowing the extension of the cell body in the direction of the stimulus source and shrinkage at the opposite end, and secondly, a decrease in the stability of the anchoring structures of the cell to the medium. Proper regulation of the two families of receptors, GPCRs and integrins ensures controlled migration. By contrast, poor regulation and integration associated pathologic migration due to cancer, chronic inflammation or vascular changes.

    The protein kinase GRK2 is a regulator of numerous GPCR which has been assigned a role of “brake” in signaling. Work codirigidopor Federico Mayor and Petronilla Penela, Center for Molecular Biology Severo Ochoa, shows that GRK2 enhances epithelial migration induced by soluble factor sphingosine-1-phosphate (a potent promigratorio increased solid tumors), participating positively in the signaling its G protein-coupled receptors, S1P1/S1P3.

    It has also been shown that interaction with GRK2 protein git1 (modulator of the cytoskeleton) is required to properly activate these receptors cascade Rac / PAK / MEK / ERK, which is key in regulating the actin cytoskeleton and cell adhesion. The work also showed that the expression of GRK2 enhances the functional relationship between S1P1/S1P3 and integrin receptors, which specifically recognize fibronectin. This relationship contributes to cell movement driven by gradients of fibronectin.

    Published on November 22, 2012 · Filed under: Bioscience; Tagged as: , , , , ,
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