Advances in microscopy techniques have revealed the details of synaptic nanodomains as defined by the segregation of specific molecules on or beneath both presynaptic and postsynaptic membranes. However, it is yet to be clarified how such segregation is accomplished without demarcating membrane and how nanodomains respond to the neuronal activity. It was recently discovered that proteins at the synapse undergo liquid–liquid phase separation (LLPS), which not only contributes to the accumulation of synaptic proteins but also to further segregating the proteins into subdomains by forming phase-in-phase structures. More specifically, CaMKII, a postsynaptic multifunctional kinase that serves as a signaling molecule, acts as a synaptic cross-linker which segregates certain molecules through LLPS in a manner triggered by Ca²⁺. Nanodomain formation contributes to the establishment of trans-synaptic nanocolumns, which may be involved in the optimization of spatial arrangement of the transmitter release site and receptor, thereby serving as a new mechanism of synaptic plasticity.

显微技术的进步揭示了突触纳米域的细节，如突触前膜和突触后膜之上或之下的特定分子的分离所定义的。然而，这种分离是如何在不划分膜的情况下完成的，以及纳米域如何对神经元活动做出反应，还有待澄清。最近发现突触处的蛋白质进行液-液相分离（LLPS），这不仅有助于突触蛋白质的积累，而且还通过形成相内结构将蛋白质进一步分离成亚结构域。更具体地说，CaMKII，一种作为信号分子的突触后多功能激酶，作为突触交联剂，以由 Ca ²⁺触发的方式通过 LLPS 分离某些分子. 纳米域的形成有助于跨突触纳米柱的建立，这可能参与了递质释放位点和受体空间排列的优化，从而成为一种新的突触可塑性机制。