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Retroposition is an important mechanism for gene origination. However, studies to elucidate the functions of new genes originated through retroposition, especially the functions related to diseases, are limited. We recently identified a mouse gene,  Rps23  retroposed gene 1 ( Rps23rg1 ), that regulates β-amyloid (Aβ) level and tau phosphorylation, two major pathological hallmarks of Alzheimer's disease (AD), and found that  Rps23rg1  originated through retroposition of the mouse ribosomal protein S23 ( Rps23 ) mRNA. Here we show that retroposition of  Rps23  mRNA occurred multiple times in different species but only generated another functionally expressed  Rps23rg1 -homologous gene,  Rps23rg2 , in mice, whereas humans may not possess functional  Rps23rg  homologs. Both  Rps23rg1  and  Rps23rg2  are reversely transcribed relative to the parental  Rps23  gene, expressed in various tissues and encode proteins that interact with adenylate cyclases. Similar to the RPS23RG1 protein, RPS23RG2 can upregulate protein kinase A activity to reduce the activity of glycogen synthase kinase-3, Aβ level and tau phosphorylation. However, the effects of RPS23RG2 are weaker than those of RPS23RG1 and such a difference could be attributed to the extra carboxyl-terminal region of RPS23RG2, which may have an inhibitory effect. In addition, we show that the transmembrane domain of RPS23RG1 is important for its function. Together, our results present a new gene family, whose products and associated signaling pathways might prevent mice from developing AD-like pathologies.

human molecular genetics

The  Rps23rg  gene family originated through retroposition of the ribosomal protein s23 mRNA and encodes proteins that decrease Alzheimer's β-amyloid level and tau phosphorylation