Researchers are now beginning to understand the many intricate mechanisms that control the trafficking and clustering of proteins important for synaptic function. Advances in imaging techniques revealed that in some cases proteins may be trafficked to contact sites as preformed complexes as opposed to individual protein molecules. Other studies showed that scaffolding proteins serve to cluster neurotransmitter receptors, and adhesion molecules, spatially restricting them to precise positions and optimizing their function. In mature neurons, scaffolding proteins may serve to modulate clustering of ion channels and other proteins, facilitating control of synaptic function and strength in response to activity, through mechanisms such as protein phosphorylation, palmitoylation, and/or degradation. Another critical finding revealed from recent investigations is that clustering of cell adhesion molecules and scaffolding proteins contributes to the specific sorting of neurotransmitter receptors that determine synapse function. Further investigation of the functional, temporal, and spatial attributes of scaffolding proteins and adhesion molecules will reveal how they work in a cooperative and integrated manner in synapse formation and at mature synapses.*

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