Activity- and memory training-induced acetylation of α-tubulin in the hippocampus

Neurobiol Learn Mem. 2020 May:171:107226. doi: 10.1016/j.nlm.2020.107226. Epub 2020 Apr 2.

Abstract

Posttranslational modifications play crucial roles in synaptic plasticity and memory formation. The important role of histone acetylation is well established in these processes. However, activity-dependent regulation of acetylation of non-histone proteins is not well understood. We previously showed that α-tubulin is acetylated in an activity-dependent manner. Here, we show that cyclin-dependent kinase 5 (CDK5) plays an important role in α-tubulin acetylation induced by KCl depolarization or N-methyl-D-aspartate stimulation of the hippocampal slices. In addition, KCl depolarization inhibits the activity of SIRT2, an α-tubulin deacetylase. The inhibitory effect of KCl on SIRT2 activity requires CDK5 activity. Furthermore, α-tubulin acetylation is enhanced by memory training in object recognition task. These results suggest that memory formation may involve α-tubulin acetylation.

Keywords: Cyclin-dependent kinase 5; Memory; Object recognition task; SIRT2; α-tubulin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Animals
  • Cyclin-Dependent Kinase 5 / metabolism
  • Excitatory Amino Acid Agonists / pharmacology
  • Hippocampus / drug effects
  • Hippocampus / metabolism*
  • Learning / drug effects
  • Learning / physiology*
  • Male
  • Memory / drug effects
  • Memory / physiology*
  • N-Methylaspartate / pharmacology
  • Rats
  • Rats, Sprague-Dawley
  • Recognition, Psychology / drug effects
  • Recognition, Psychology / physiology*
  • Sirtuin 2 / metabolism
  • Tubulin / metabolism*

Substances

  • Excitatory Amino Acid Agonists
  • Tubulin
  • N-Methylaspartate
  • Cyclin-Dependent Kinase 5
  • Sirtuin 2