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Fragile X mental retardation protein (FMRP) binds to and regulates the translation of amyloid-β protein precursor ( App ) mRNA, but the detailed mechanism remains to be determined. Differential methylation of  App  mRNA could underlie FMRP binding, message localization and translation efficiency. We sought to determine the role of FMRP and N 6 -methyladeonsine (m 6 A) on nuclear export of  App  mRNA. We utilized the m 6 A dataset by Hsu and colleagues to identify m 6 A sites in  App  mRNA and to determine if the abundance of message in the cytoplasm relative to the nucleus is altered in  Fmr1  knockout mouse brain cortex. Given that processing of APP to Aβ and soluble APP alpha (sAPPα) contributes to disease phenotypes, we also investigated whether  Fmr1   KO   associates with nuclear export of the mRNAs for APP protein processing enzymes, including β-site amyloid cleaving enzyme (Bace1), A disintegrin and metalloproteinases (Adams), and presenilins (Psen).  Fmr1  KO  did not alter the nuclear/cytoplasmic abundance of  App  mRNA. Of 36 validated FMRP targets, 35 messages contained m 6 A peaks but only  Agap2  mRNA was selectively enriched in  Fmr1   KO   nucleus. The abundance of the APP processing enzymes  Adam9  and  Psen1  mRNA, which code for a minor alpha-secretase and gamma-secretase, respectively, were selectively enriched in wild type cytoplasm.

FMRP Regulates the Nuclear Export of Adam9 and Psen1 mRNAs: Secondary Analysis of an N6-Methyladenosine Dataset