ATP6V0d2 mediates leucine-induced mTORC1 activation and polarization of macrophages.
Li, Pingfei; Deng, Xiaofei; Luo, Jing; Chen, Yufei; Bi, Guoyu; Gong, Feili; Wei, Zhengping; Liu, Na; Li, Huabin; Laurence, Arian; Yang, Xiang-Ping.
; 2019 May 27.
Artigo em Inglês | MEDLINE | ID: mdl-31134526
Evidence for a role for Sestrin1 in mediating leucine-induced activation of mTORC1 in skeletal muscle.
Coordination of the leucine-sensing Rag GTPase cycle by leucyl-tRNA synthetase in the mTORC1 signaling pathway.
mTORC1 is involved in the regulation of branched-chain amino acid catabolism in mouse heart.
ERK and Akt signaling pathways function through parallel mechanisms to promote mTORC1 signaling.
PAQR3 augments amino acid deprivation-induced autophagy by inhibiting mTORC1 signaling.
Ursolic acid inhibits leucine-stimulated mTORC1 signaling by suppressing mTOR localization to lysosome.
Roles of Mitogen-Activating Protein Kinase Kinase Kinase Kinase-3 (MAP4K3) in Preterm Skeletal Muscle Satellite Cell Myogenesis and Mammalian Target of Rapamycin Complex 1 (mTORC1) Activation Regulation.
mTORC1 Activator SLC38A9 Is Required to Efflux Essential Amino Acids from Lysosomes and Use Protein as a Nutrient.
Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway.
Inhibition of mTORC1 by astrin and stress granules prevents apoptosis in cancer cells.