Detection of focal adhesion kinase activation at membrane microdomains by fluorescence resonance energy transfer
- Detection of focal adhesion kinase activation at membrane microdomains by fluorescence resonance energy transfer
- 성지혜; Mingxing Ouyang; Taejin Kim; Jie Sun; Po-Chao Wen; Shaoying Lu; Yue Zhuo; Nicholas M. Llewellyn; David D. Schlaepfer; Jun-Lin Guan; Shu Chien; Yingxiao Wang
- Issue Date
- Nature Communications
- VOL 2, NO 406, 1-9
- Proper subcellular localization of focal adhesion kinase (FAK) is crucial for many cellular processes. It remains, however, unclear how FAK activity is regulated at subcellular compartments. To visualize the FAK activity at different membrane microdomains, we develop a fluorescence resonance energy transfer (FRET)-based FAK biosensor, and target it into or outside of detergent-resistant membrane (DRM) regions at the plasma membrane. Here we show that, on cell adhesion to extracellular matrix proteins or stimulation by platelet-derived growth factor (PDGF), the FRET responses of DRM-targeting FAK biosensor are stronger than that at non-DRM regions, suggesting that FAK activation can occur at DRM microdomains. Further experiments reveal that the PDGF-induced FAK activation is mediated and maintained by Src activity, whereas FAK activation on cell adhesion is independent of, and in fact essential for the Src activation. Therefore, FAK is activated at membrane microdomains with distinct activation mechanisms in response to different physiological stimuli.
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