Long-term potentiation (LTP) of synaptic transmission is considered to be a cellular counterpart of learning and memory. Activation of postsynaptic NMDA type glutamate receptor (NMDA-R) induces trafficking of AMPA type glutamate receptors (AMPA-R) and other proteins to the synapse in sequential fashion. At the same time, the dendritic spine expands for long-term and modulation of actin underlies this (structural LTP or sLTP). How these changes persist despite constant diffusion and turnover of the component proteins have been the central focus of the current LTP research. Signaling triggered by Ca²⁺-influx via NMDA-R triggers kinase including Ca²⁺/calmodulin-dependent protein kinase II (CaMKII). CaMKII can sustain longer-term biochemical signaling by forming a reciprocally-activating kinase-effector complex with its substrate proteins including Tiam1, thereby regulating persistence of the downstream signaling. Furthermore, activated CaMKII can condense at the synapse through the mechanism of liquid-liquid phase separation (LLPS). This increases the binding capacity at the synapse, thereby contributing to the maintenance of enlarged protein complexes. It may also serve as the synapse tag, which captures newly synthesized proteins.

突触传递的长时程增强 (LTP) 被认为是学习和记忆的细胞对应物。突触后 NMDA 型谷氨酸受体 (NMDA-R) 的激活诱导 AMPA 型谷氨酸受体 (AMPA-R) 和其他蛋白质以顺序方式向突触转运。同时，树突棘长期扩张，肌动蛋白的调节是其基础（结构 LTP 或 sLTP）。尽管成分蛋白不断扩散和更新，这些变化如何持续存在是当前 LTP 研究的中心焦点。由 Ca ²⁺流入通过 NMDA-R 触发的信号转导触发包括 Ca ^{2+在内的激酶}/钙调蛋白依赖性蛋白激酶 II (CaMKII)。CaMKII 可以通过与其底物蛋白（包括 Tiam1）形成相互激活的激酶效应复合物来维持更长期的生化信号传导，从而调节下游信号传导的持久性。此外，活化的 CaMKII 可以通过液-液相分离 (LLPS) 机制在突触处凝聚。这增加了突触的结合能力，从而有助于维持扩大的蛋白质复合物。它也可以作为突触标签，捕获新合成的蛋白质。