Monther Abu-Remaileh
Worked out how to isolate lysosomes fast enough to measure what is inside them, and found that mTOR controls what gets out
Assistant Professor of Chemical Engineering and of Genetics, Stanford University · postdoctoral research, Whitehead Institute and MIT, in David Sabatini's laboratory (to 2019) · PhD in Molecular Genetics, The Hebrew University of Jerusalem (2014)
Abu-Remaileh Lab, Stanford University (Stanford, California, USA) ↗ Bluesky@abu-remaileh.bsky.social ↗ ORCID0000-0003-3772-0477 ↗
Portrait: Sarafan ChEM-H, Stanford University
The lysosome is where mTORC1 is switched on, so what is inside it matters — but lysosomal metabolites turn over in seconds, and conventional fractionation is far too slow to catch them. ABU2017 solves the measurement problem first: a rapid immunoprecipitation method that pulls lysosomes out of a cell in minutes, followed by metabolite profiling of the isolated organelles.
The biology that follows reverses an arrow the Atlas draws. Blocking the v-ATPase raised the luminal concentration of most metabolites but left most essential amino acids alone. Nutrient starvation did change them, and the effect traced back to mTOR: inhibiting mTOR strongly reduced the efflux of essential amino acids from the lysosome, converting the organelle into a store. So the lysosome is not only the platform that activates mTORC1; mTORC1 also decides what the lysosome releases.
His laboratory at Stanford works on how cells and organisms adapt to metabolic stress, with the lysosome at the centre and with applications in cancer and in neurodegeneration, including lysosomal storage disorders.
Milestones in the Atlas
| Year | Evidence | Study |
|---|---|---|
| 2017 | M | Lysosomal metabolomics reveals V-ATPase- and mTOR-dependent regulation of amino acid efflux from lysosomes ABU2017 First author: rapid lysosome isolation plus metabolomics shows mTOR controls the efflux of essential amino acids from the lysosome. |