The Rag-family GTPases, known activators of TOR complex 1 (TORC1), also function as attenuator that prevents deregulated hyperactivation of TORC1 signaling.

The H+ influx coupled to nutrient uptake and the plasma membrane H+-ATPase are central actors of the activation of target of rapamycin complex 1 (TORC1) in budding yeast Saccharomyces cerevisiae..

The ZNRF2 enzyme helps the mTOR protein complex to sense amino acid levels and regulate mammalian cell growth.

Signaling pathway mTOR can sense its principal activator amino acid arginine via a different mechanism than that previously described for other amino acids.

Activation by amino acids causes mTORC1 to translocate transiently to the lysosomal surface.

Sea3, a presumed subunit of the GATOR2 complex in fission yeast, is required for the GATOR1 function that attenuates TORC1 in parallel with the TSC complex and Gcn2 kinase.

Protein kinase A (PKA) phosphorylates Raptor and inhibits mammalian target of rapamycin complex 1 (mTORC1) activity.

A new mechanism linking lysosomes to mTOR regulation and synaptic plasticity involves p18 ubiquitination by Ube3a, and underlies some of the pathology observed in Angelman syndrome.

Discovery of new Snf1/AMPK targets in the TORC1 pathway highlights the complex, multilayered crosstalk between major signaling pathways in the regulation of nutrient deprivation sensing.

The multipronged chemical biology approach unraveled a novel mechanism by which mTOR is regulated by the second messenger calcium.