Maria A Frias
Cancer biologist who did her doctoral research on mTORC2 in David Sabatini's lab and now teaches biology at St. Francis College in Brooklyn, while continuing work with David Foster on how the lipid phosphatidic acid controls mTOR
Assistant Professor and Chair of Biology, St. Francis College, Brooklyn (since 2021) · postdoctoral research, The Rockefeller University and Hunter College, City University of New York (David Foster lab) · PhD in Cancer Biology, Medical School of the University of Lisbon (2008), with the research done in David Sabatini's lab at the Whitehead Institute
Department of Biology, St. Francis College (Brooklyn, New York, USA) ↗ Lab lineagetrained under David M. Sabatini →
mTOR, the cell's central growth kinase, works inside two different protein complexes. mTORC1 is the one rapamycin blocks; mTORC2 was the less understood partner, and one of its main jobs is to switch on Akt, a kinase that keeps cells alive and responds to insulin. In 2006, as first author of a Current Biology paper from David Sabatini's lab (FRI2006), Maria Frias showed in human cells that a protein called mSin1 is needed to build mTORC2 and for mTORC2 to add a phosphate to Akt at serine 473. The mSin1 gene makes several versions of the protein, and the paper found that three of them each sit in a distinct form of mTORC2, so there is more than one mTORC2 in a cell.
Frias did this work as a doctoral student from Portugal. Her official faculty pages say her PhD in Cancer Biology was awarded by the Medical School of the University of Lisbon in 2008, with the research carried out in the Sabatini lab at the Whitehead Institute and funded by a Portuguese government fellowship. She then did postdoctoral research at The Rockefeller University and at Hunter College of the City University of New York, and received a grant for a Master of Science in Clinical and Translational Investigation at Weill Cornell Medicine.
At Hunter College she worked with David Foster on phosphatidic acid, a membrane lipid that binds mTOR and helps hold its complexes together. PubMed lists her on papers from that group on how cells keep phosphatidic acid levels steady for mTOR (2014), on the two-way link between the energy sensor AMPK and phospholipase D (2015), on why rapamycin works at different doses in different settings (2016), on glutamine switching on mTORC1 through phospholipase D (2018), on cancer cells that resist rapamycin when RB and CDKN2A are both mutated (2021), and a 2023 review on how phosphatidic acid regulates mTOR. She joined St. Francis College in Brooklyn in 2021 and is Assistant Professor and Chairperson of Biology there; her stated research aim is to work out what controls mTORC1, how cancer cells exploit it and which drugs could block it.
Milestones in the Atlas
A selection, not a full bibliography: only papers that meet the Atlas inclusion criteria.
| Year | Evidence | Study |
|---|---|---|
| 2006 | M | mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define three distinct mTORC2s FRI2006 First author: showed in human cells that mSin1 is required to assemble mTORC2 and for Akt phosphorylation, and that mSin1 variants define three distinct mTORC2s. |
Co-authors in the Atlas 2
People with a profile here who share at least one study with Maria A Frias.
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- Carson C. Thoreen Used Torin1, one of the first ATP-competitive mTOR inhibitors, to reveal functions of mTORC1 that rapamycin cannot block. He then showed that mTORC1 controls translation of mRNAs for the protein-making machinery mainly through the 4E-BP proteins
- David M. Sabatini Identified mTOR (as RAFT1) in 1994. His lab then mapped much of the machinery around it: raptor and rictor at the core of mTORC1 and mTORC2, the Rag–Ragulator system that docks mTORC1 on the lysosome, and the sensors that detect leucine, arginine and SAM
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