Acetylation of calmodulin regulates synaptic plasticity and fear learning.

ABSTRACT: Synaptic plasticity is critical for brain function, including learning and memory. It is regulated by gene transcription and protein synthesis as well as posttranslational modifications at synapses. Although protein acetylation has been shown to be involved in the regulation of synaptic plasticity, this was mainly for histone protein acetylation. To investigate whether acetylation of nonhistone proteins is important for synaptic plasticity, we analyzed mouse brain acetylome and found that calmodulin (CaM), a ubiquitous Ca²⁺ sensor, was acetylated on three lysine residues, which were conserved across species. NMDA receptor-dependent long-term potentiation (LTP) is considered the most compelling form of synaptic plasticity. During LTP induction, activation of NMDA receptor trigger

SUBMITTER: Zhang HL 

PROVIDER: S-EPMC8383114 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature