Title : Mechanical Stretch Induces mTOR Recruitment and Activation at the Phosphatidic Acid-Enriched Macropinosome in Muscle Cell.

Pub. Date : 2019

PMID : 31139627






6 Functional Relationships(s)
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1 Mechanical Stretch Induces mTOR Recruitment and Activation at the Phosphatidic Acid-Enriched Macropinosome in Muscle Cell. Phosphatidic Acids mechanistic target of rapamycin kinase Homo sapiens
2 Mechanical load has been well-appreciated to induce mTOR activation that leads to skeletal muscle growth through phospholipase D (PLD) activity and phosphatidic acid (PA) production. Phosphatidic Acids mechanistic target of rapamycin kinase Homo sapiens
3 Mechanical load has been well-appreciated to induce mTOR activation that leads to skeletal muscle growth through phospholipase D (PLD) activity and phosphatidic acid (PA) production. Phosphatidic Acids mechanistic target of rapamycin kinase Homo sapiens
4 While PA produced by PLD1 is critical for mTOR activation upon mitogenic stimulation at the lysosome, it is unclear where PA is produced upon mechanical stimulation in skeletal muscle. Phosphatidic Acids mechanistic target of rapamycin kinase Homo sapiens
5 Furthermore, mTOR is recruited to the PA-enriched macropinosome, and its downstream signaling is activated. Phosphatidic Acids mechanistic target of rapamycin kinase Homo sapiens
6 Our findings reveal the underpinning of mechanical activation of mTOR signaling, and more importantly, the stretch-induced PA-macropinosome as a new platform for mTOR activation. Phosphatidic Acids mechanistic target of rapamycin kinase Homo sapiens