This technique is commonly used in conjunction with green fluorescent protein (GFP) fusion proteins, where the studied protein is fused to a GFP.  When excited by a specific wavelength of light, the protein will fluoresce.  When the protein that is being studied is produced with the GFP, then the fluorescence can be tracked.  Photodestroying the GFP, and then watching the repopulation into the bleached area can reveal information about protein interaction partners, organelle continuity and protein trafficking.
If after some time the fluorescence doesn't reach the initial level anymore, then some part of the fluorescence is caused by an immobile fraction (that cannot be replenished by diffusion).  Similarly, if the fluorescent proteins bind to static cell receptors, the rate of recovery will be retarded by a factor related to the association and disassociation coefficients of binding.  This observation has most recently been exploited to investigate protein binding. Similarly, if the GFP labeled protein is constitutively incorporated into a larger complex, the dynamics of fluorescence recovery will be characterized by the diffusion of the larger complex.