CaMKII monomers are sufficient for GluN2B binding, co-condensation, and synaptic potentiation.

CaMKII monomers can bind GluN2B, co-condense, and induce synaptic potentiation, revealing a new mechanism for LTP independent of holoenzyme formation.

• Why it matters: Understanding how CaMKII interacts with GluN2B is crucial for deciphering the molecular basis of synaptic plasticity and memory formation, yet the role of monomers has been unclear.
• What they did: The study examined full-length and truncated CaMKII monomers, demonstrating that full-length monomers bind GluN2B and form condensates, while truncated monomers do not, despite both potentiating synapses under specific conditions.
• The result: Findings show that CaMKII monomers, especially when Ca2+-independent, can facilitate LTP by generating autonomous activity, highlighting a monomer-based pathway for synaptic strengthening.