NCOA5 is a master regulator of amino acid-induced mTOR activation and β-casein synthesis in bovine mammary epithelial cells.

In this study, we explored the role and molecular mechanism of NCOA5 in amino acid-induced activation of the mechanistic target of rapamycin (mTOR) and milk protein synthesis in bovine mammary epithelial cells (BMECs). Methionine (Met) and leucine (Leu) significantly up-regulated the expression of NCOA5. NCOA5 overexpression increased mTOR phosphorylation and β-casein synthesis, whereas its knockdown exhibited the opposite effects. Furthermore, inhibition of phosphatidylinositol 3-kinase (PI3K) completely abolished the stimulatory effects of Met and Leu on NCOA5 expression. ChIP-qPCR analysis detected that NCOA5 bound to the mTOR promoter, and this interaction was enhanced by the stimulation of Met and Leu. These above data reveal that NCOA5 is a key regulator of amino acid-induced PI3K-mediated mTOR activation and β-casein synthesis in BMECs.
PMID: 32736675 [PubMed - as supplied by publisher]

Source: Biochemical and Biophysical Research communications - August 3, 2020 Category: Biochemistry Authors: Yuan X, Zhang L, Cui Y, Yu Y, Gao X, Ao J Tags: Biochem Biophys Res Commun Source Type: research