Rps23rg1, also part of the Rps23rg gene family which originated through retroposition of the ribosomal protein s23 mRNA, is implicated in multiple biological processes relevant to neurodegenerative diseases. It interacts with adenylate cyclases, upregulates protein kinase A activity, and reduces glycogen synthase kinase-3 activity, thus affecting pathways related to Alzheimer's disease (AD) and tauopathies [3].

In Rps23rg1 knockout (KO) mice, there are significant phenotypic changes. These include retarded axon outgrowth, elevated p35 and p25 protein levels, increased tau phosphorylation at major Cdk5 phosphorylation sites, severe memory deficits, and impairment of postsynaptic structure and function with reduced levels of postsynaptic densities-93 and-95 (PSD-93 and PSD-95) [1,2]. These phenotypes suggest that Rps23rg1 is involved in maintaining synaptic integrity, regulating tau phosphorylation, and axon outgrowth [1,2].

In conclusion, Rps23rg1 plays essential roles in maintaining synaptic function, regulating tau phosphorylation, and axon outgrowth. Studies using Rps23rg1 KO mouse models have significantly contributed to understanding its functions in neurodegenerative diseases like AD and tauopathies, providing potential therapeutic targets for these disorders.