Abstract
Focal adhesion kinase (FAK) and paxillin are involved in focal adhesion (FA) disassembly and formation, which can regulate cell migration, intracellular signaling, and remodeling of actin filaments. We used time‐lapse double‐color imaging to monitor concurrently the spatial‐temporal dynamics of FAK and paxillin in live endothelial cells (ECs) co‐transfected with GFP‐FAK and DsRed‐paxillin, and the fluorescence intensities (FI) of paxillin and FAK at FAs were determined in cell front, center and rear. The mean FAK/Paxillin FI ratio is highest at cell front (mean±SEM: 4.73±0.48), near 1 at cell center (0.95±0.11), and lowest at cell rear (0.64±0.05) (P<0.01). Determination of the time difference between the assemblies of FAK and paxillin at FAs in lamellipodial protrusion (LP) showed that FAK assembly occurs ahead of that of paxillin at individual FAs. Computational analysis indicates that FAK reaches its maximum intensity earlier than paxillin by about 4 min. The assembly of FAK is at LP ahead of paxillin Indicates that, while both molecules play important roles in modulating FA dynamics during cell migration, FAK promotes FA formation ahead of paxillin at the cell leading edge. This work was supported by NHLBI Research Grants HL‐104402 and HL‐106579 (S.C.).
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