The objectives of this study are twofold: (1) to establish the optimal conditions for ultrafast PALM of mEos3.2, ultrafast dSTORM of HMSiR, and their simultaneous imaging and (2) to apply these methods and ultrafast SFMI (its development is described in the companion paper) to elucidate the FA architecture and protein dynamics in the FA. The second purpose, together with the previous results, is summarized in the figure. (A and B) Both the apical (dorsal) PM (A, left) and basal (ventral) PM (A, right) are compartmentalized in a nearly identical manner by actin-based membrane-skeleton meshes (fences; brown mesh in B) and rows of transmembrane-protein pickets anchored to and aligned along the actin fence (blue molecules in B), which induce the hop diffusion of virtually all membrane molecules in both the apical and basal PM (B). See the companion paper for these results. (C) Three fundamental questions about the FA molecular organization addressed here are as follows: (1) the characteristics of the FA-protein clusters/oligomers/islands, (2) the higher-order organizations of the FA-protein clusters/oligomers/islands, and (3) the possibility that the fluid membrane part in the FA is compartmentalized, like the bulk basal PM. For details, see D. (D) The three models of the molecular organization in the FA proposed previously (a–c) and the two new models (d and e) proposed here. The new models incorporate the formation of loose clusters of FA-protein islands (d) plus the compartmentalization of the fluid membrane part in the FA (e).