Estela Jacinto
Co-discovered mammalian mTORC2 as a postdoc in Michael Hall's lab, showing that it controls the actin cytoskeleton and is insensitive to rapamycin. Her Rutgers lab, with Bing Su's group, was among those that found SIN1 holds mTORC2 together and studies how both mTOR complexes control metabolism
Professor of Biochemistry & Molecular Biology, Rutgers Robert Wood Johnson Medical School · postdoc, Biozentrum, University of Basel (Michael Hall lab) · PhD, UC San Diego
Jacinto Lab, Rutgers RWJMS (Piscataway, New Jersey, USA) ↗ Lab lineagetrained under Michael N. Hall → ORCID0000-0001-7118-1759 ↗
Portrait: Jacinto Lab, Rutgers
Estela Jacinto did her postdoctoral training with Michael Hall at the Biozentrum in Basel, one of the labs that pioneered TOR biology, where she helped identify and characterize the second, rapamycin-insensitive mTOR complex, mTORC2.
Her 2004 and 2006 papers, alongside parallel work from the Sabatini lab and others, helped establish that mTORC2 contains rictor and the scaffold protein SIN1/MIP1, and that this complex — distinct from the raptor-containing mTORC1 — controls the actin cytoskeleton and phosphorylates Akt at a site required for its full activation. That work set up mTORC2 as a parallel signalling arm alongside mTORC1, now studied for its own roles in metabolism, cancer and immunity. She now runs her own lab at Rutgers, studying how mTORC1 and mTORC2 together shape metabolism in cancer, aging and immune cells.
The timeline below follows Jacinto's contributions gathered in this Atlas.
Milestones in the Atlas
A selection, not a full bibliography: only papers that meet the Atlas inclusion criteria.
| Year | Evidence | Study |
|---|---|---|
| 2002 | M | Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control LOE2002 Defined two distinct TOR complexes, only one rapamycin-sensitive, founding the TORC1/TORC2 paradigm. |
| 2004 | M | Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive JAC2004 Shows mammalian TOR complex 2 (mTORC2) controls the actin cytoskeleton and, unlike mTORC1, is not directly inhibited by rapamycin. |
| 2006 | M | SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity JAC2006 Shows SIN1/MIP1 is required to maintain rictor-mTOR (mTORC2) complex integrity and its control of Akt phosphorylation and substrate specificity. |
| 2008 | M | The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C FAC2008 Senior author: shows mTORC2 phosphorylates the turn motif of Akt and PKC, which they need to fold correctly and stay stable. |
| 2021 | R | Regulation and metabolic functions of mTORC1 and mTORC2 SZW2021 Reviews the distinct regulation and metabolic functions of mTORC1 and mTORC2. |
Co-authors in the Atlas 6
People with a profile here who share at least one study with Estela Jacinto.
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- Bing Su 2 shared studies Immunologist who studies how mTOR and MAPK signaling shape immune regulation and vascular function, and senior author of the study showing that SIN1 is a core part of mTORC2.
- Michael N. Hall 2 shared studies Discovered TOR in yeast in 1991 and established it as a central controller of cell growth that responds to nutrients. His lab later showed that TOR works in two distinct complexes, TORC1 and TORC2, only one of which is blocked by rapamycin
- Robbie Loewith 2 shared studies Showed, as first author in Michael Hall's lab, that yeast TOR exists as two distinct complexes, the basis of the TORC1/TORC2 framework
- Angelia Szwed Lead author, from Estela Jacinto's Rutgers lab, of a long Physiological Reviews article on how the two mTOR complexes are controlled and what they do in metabolism
- Markus A. Rüegg Neurobiologist at the Biozentrum of the University of Basel who studies how muscles and the nerve connections that drive them develop, age and fail, including the role of mTOR signalling in muscle.
- Valeria Facchinetti First author of the study showing that mTORC2 phosphorylates the turn motif of Akt and conventional PKC as the proteins are made, which helps them fold and stay stable
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