Torin1
ATP-competitive ('active-site') mTOR inhibitor. Unlike rapamycin, it blocks the kinase active site directly and so fully inhibits BOTH complexes - the tool that revealed rapamycin-resistant functions of mTORC1.
A lab-only drug that blocks mTOR directly at its 'engine room' (the active site), so - unlike rapamycin - it shuts down both mTOR complexes completely. It was a key tool for discovering what rapamycin-resistant mTOR functions look like.
ATP-competitive ('active-site') mTOR inhibitor. Unlike rapamycin, it blocks the kinase active site directly and so fully inhibits BOTH complexes - the tool that revealed rapamycin-resistant functions of mTORC1.
TL;DR. Torin1 appears in 3 curated studies in Oliver's mTOR Atlas: 3 at the molecular level (cells, biochemistry, structure). No study in people is recorded for it in the Atlas yet.
Evidence at a glance
| Evidence | What it means | Studies |
|---|---|---|
| M | Molecular — cells, biochemistry, structure | 3 |
No direct human evidence in the Atlas for this entity yet — everything below rests on animal or molecular work.
Studies
| Year | Evidence | Study |
|---|---|---|
| 2017 | M | Lysosomal metabolomics reveals V-ATPase- and mTOR-dependent regulation of amino acid efflux from lysosomes ABU2017 Turns the lysosome from a place where mTORC1 is switched on into something mTORC1 also controls: inhibiting mTOR strongly reduces the efflux of most essential amino acids out of the lysosome, so the organelle becomes a store rather than a source. Measured directly by rapidly isolating lysosomes and profiling their contents, which is why the claim is about concentrations inside the organelle and not inferred from signalling readouts. Boundary: one human cell line, acute pharmacological inhibition. |
| 2013 | M | mTORC1 phosphorylation sites encode their sensitivity to starvation and rapamycin KAN2013 Each mTORC1 phosphorylation site has its own intrinsic 'substrate quality'. Good substrates stay phosphorylated when mTORC1 is partly inhibited by rapamycin or starvation, poor ones drop out first, and changing a few residues around a site shifts its sensitivity in cells. One level of mTORC1 activity can therefore produce different output profiles. |
| 2009 | M | An ATP-competitive mammalian target of rapamycin inhibitor reveals rapamycin-resistant functions of mTORC1 THO2009 Dropped a bombshell: rapamycin does NOT fully block mTORC1. Using Torin1 (which jams the active site directly), the authors showed rapamycin leaves important mTORC1 jobs running - notably 4E-BP1 phosphorylation and autophagy suppression. This reframed a decade of rapamycin experiments and launched the search for complete inhibitors. |
Related entities
Thank you. Your answer was counted anonymously.