LTP expression mediated by autonomous activity of GluN2B-bound CaMKII

Cell Rep. 2024 Oct 22;43(10):114866. doi: 10.1016/j.celrep.2024.114866. Epub 2024 Oct 11.

Abstract

Learning and memory are thought to require the induction and maintenance of long-term potentiation (LTP) of synaptic strength. LTP induction requires the Ca2+/calmodulin-dependent protein kinase II (CaMKII) but for structural rather than enzymatic functions. We show that the relevant structural function is regulated by CaMKII binding to the NMDA-type glutamate receptor subunit GluN2B. This binding directly generates Ca2+-independent autonomous CaMKII activity, and we show that this enzymatic activity is dispensable for LTP induction (within 5 min) but required for a subsequent LTP phase (within 15 min). This requirement for CaMKII activity provides an objective temporal definition for the intermediary phase of LTP expression. Later LTP maintenance may still require structural functions of GluN2B-bound CaMKII but not the resulting enzymatic CaMKII activity or their co-condensation. Thus, autonomous CaMKII activity mediates post-induction LTP but (1) via GluN2B binding, not T286 autophosphorylation, and (2) during the intermediary expression phase rather than for long-term maintenance.

Keywords: CP: Molecular biology; CP: Neuroscience; CaMKII; GluN2B; LTP expression; LTP induction; LTP maintenance; NMDAR; binding; condensation.

MeSH terms

  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2* / metabolism
  • Hippocampus / metabolism
  • Humans
  • Long-Term Potentiation* / physiology
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Phosphorylation
  • Protein Binding
  • Receptors, N-Methyl-D-Aspartate* / metabolism

Substances

  • Receptors, N-Methyl-D-Aspartate
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • NR2B NMDA receptor