Dynamics of myristoylated amino-terminal domain of Src in the plasma membrane of mechano-stimulated cells studied by single molecule imaging

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Src is a critical signaling molecule for mechanotransduction. Mechanical stimuli applied on the cell can induce a rapid Src activation, but it remains largely unknown how mechanical stimuli activates Src molecules. Here, we observed fluorescently labeled myristoylated amino terminus of Src in the plasma membrane of living cells at the single molecule level to examine the role of lipid moiety of the amino terminus of Src on its dynamics and activation. Most probes were observed to diffuse rapidly in the membrane, but that significant fraction of the molecules exhibited temporal immobilization. We also found that the immobilization of them occurred frequently in the proximity of focal adhesions (FAs), and that it was mechano- and cholesterol-dependent. These results suggest that lipid moiety of the amino terminus of Src may play a critical role in the dynamics and activation of Src molecules around FAs through the interaction with lipid micro domains of the plasma membrane.