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Related Experiment Video

Updated: Aug 26, 2025

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Synaptic memory survives molecular turnover.

Joel Lee1, Xiumin Chen1, Roger A Nicoll1,2

  • 1Department of Cellular and Molecular Pharmacology, University of California at San Francisco, San Francisco, CA 94158.

Proceedings of the National Academy of Sciences of the United States of America
|October 10, 2022
PubMed
Summary

Long-term potentiation (LTP) and memory persist despite protein turnover. Newly synthesized Ca2+/calmodulin-dependent kinase II (CaMKII) molecules acquire activity from existing active CaMKII, maintaining synaptic memory traces.

Keywords:
CaMKIImemorysynapse

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Area of Science:

  • Neuroscience
  • Cellular Biology
  • Molecular Biology

Background:

  • Ca2+/calmodulin-dependent kinase II (CaMKII) activation is crucial for long-term potentiation (LTP), a cellular model of learning and memory.
  • The mechanism by which synaptic plasticity and memory survive protein turnover, especially CaMKII, is not well understood.

Purpose of the Study:

  • To investigate how synaptic memory traces are maintained over time despite the turnover of key proteins like CaMKII.
  • To explore the role of constitutive CaMKII activity in preserving memory in the absence of continuous stimulation.

Main Methods:

  • Utilized slice culture preparations to maintain neuronal function over an extended period (2 weeks).
  • Investigated CaMKII activity in the absence of Ca2+ stimulation to assess its persistence.
  • Examined the stability of CaMKII activity beyond the protein's natural turnover rate.

Main Results:

  • Constitutive Ca2+-independent CaMKII activity, established before slice preparation, acts as a lasting memory trace at synapses.
  • This persistent CaMKII activity remained stable for 2 weeks in slice culture, even without Ca2+ stimulation.
  • The stability of CaMKII activity extended well beyond the typical turnover period of the CaMKII protein itself.

Conclusions:

  • Propose a model where newly synthesized CaMKII molecules acquire activity from pre-existing active CaMKII molecules.
  • This activity transfer mechanism allows for the maintenance of synaptic memory traces through protein turnover.
  • Suggests a novel pathway for enduring memory formation at the molecular level.