The precision of signal transmission in chemical synapses is highly dependent on the structural alignment between pre- and postsynaptic components. The thermal agitation of transmembrane signaling molecules by surrounding lipid molecules and activity-driven changes in the local protein interaction affinities indicate a dynamic molecular traffic of molecules within synapses. The observation of local protein surface dynamics starts to be a useful tool to determine the contribution of intracellular and extracellular structures in organizing a plastic synapse. Local rearrangements by lateral diffusion in the synaptic and perisynaptic membrane induce fast density changes of signaling molecules and enable the synapse to change efficacy in short time scales. The degree of lateral mobility is restricted by many passive and active interactions inside and outside the membrane. AMPAR at the glutamatergic synapse are the best explored receptors in this respect and reviewed here as an example molecule. In addition, transsynaptic adhesion molecule complexes also appear highly dynamically in the synapse and do further support the importance of local surface traffic in subcellular compartments like synapses.