Reversibly photoswichable fluorescent proteins (RSFPs) are now indispensable tools for superresolution imaging of physiological events by means of nanoscopies. However their application to observe protein dynamics has still been limited because of the slow switching behavior. In addition, the poor photostability perturbs long term image acquisition. To overcome these problems, we have developed a RSFP which has the fastest switching speed and the highest photostability among the RSFPs developed to date. By applying the novel RSFP to photoactivated localization microscopy, we could observe nanoscale dynamics of paxilin expressing in the focal adhesion. Simultaneous laser illumination for both on- and off-photoswitching could induce effective blinking behavior enabling to perform photochromic stochastic optical fluctuation imaging of actin structure. Moreover, super-resolved imaging of vimentin could be obtained by conducting reversible saturable optical fluorescence transition nanoscopy using a simplified optics and extremely low laser power than before. This novel RSFP would open the door as a fusion tag to superresolve biomolecular dynamics within the live cells.