1D15 アクチン結合タンパク質の動態に関する研究

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  • 石川 晃大
    名古屋工業大学大学院機能工学専攻
  • 松井 翼
    名古屋工業大学大学院共同ナノメディシン科学専攻
  • 出口 真次
    名古屋工業大学大学院共同ナノメディシン科学専攻

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  • 1D15 Analysis on an actin binding protein

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Actin cytoskeleton plays critical roles in many aspects of cell functions, such as cell movement, cell division, shape maintenance, contractile force generation, and so on. Actin organization is regulated in a spatiotemporal manner by various actin-related proteins. Transgelin 1 is a 22 kDa actin binding protein of calponin family, and is known as a molecular marker for differentiated contractile smooth muscle cells. Transgelin 1 is thought to act as an actin cross-linker and stabilizer. However, the details of transgelin 1 dynamics remain unknown. In this study, we characterize transgelin 1 dynamics with fluorescence recovery after photobleaching (FRAP). First, we consider the spatial regulation of transgelin 1 dynamics. Our result reveals that transgelin 1 molecules are highly diffusive at stress fibers located in the central portion of the cell and have higher affinity to actin filaments in peripheral stress fibers than those in central stress fibers. A previous study reported that actin binding of transgelin 1 is negatively regulated by phosphorylation of serine residue Ser181. Constructing transgelin 1 phosphomimic and nonphosphorylatable mutants, we evaluate the effect of phosphorylation of Ser181 in transgelin 1. Time constants of recovery curves were not significantly different among transgelin 1 mutants. The results indicate that the phosphorylation at Ser181 does not affect transgelin 1 dynamics.

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