Oliver's mTOR Atlas Evidence Platform
Reading level
Mode

Stuart L. Schreiber

Co-discovered mTOR in 1994 (his group called it FRAP) as the mammalian target of the FKBP12–rapamycin complex, and helped found chemical biology as a field

co-founder, Arena BioWorks (2024–2025; closed November 2025) · Morris Loeb Professor of Chemistry and Chemical Biology, Harvard University (from 1988, now Emeritus) · co-founder of the Broad Institute · HHMI Investigator (Emeritus) · assistant professor, Yale University (1980) · PhD, Harvard University (Robert B. Woodward, then Yoshito Kishi) · BA in chemistry, University of Virginia

Faculty profile, Harvard University (Cambridge, Massachusetts, USA) ↗

Stuart L. Schreiber Portrait: Broad Institute

In 1994, Schreiber's lab purified the mammalian protein that binds the immunosuppressant complex FKBP12–rapamycin — naming it FRAP, later renamed mTOR — and showed it was the human homolog of yeast TOR1/TOR2, the genes originally implicated in rapamycin's growth-arresting effects. Two years later, his group solved the crystal structure of FKBP12–rapamycin bound to mTOR's FRB domain, revealing the atomic mechanism: a single rapamycin molecule sits in the interface and plugs into two separate hydrophobic pockets, one on FKBP12 and one on FRB, physically gluing the two proteins together. That structure became a founding example of a 'molecular glue' — a small molecule that works not by blocking a single active site but by forcing two proteins into an unnatural complex, a concept that now underlies molecular-glue degraders; related induced-proximity drugs such as PROTACs use a different, bifunctional design.

Schreiber trained in organic synthesis at Harvard, first under Robert B. Woodward and then Yoshito Kishi after Woodward's death, before starting his own lab at Yale in 1980 and returning to Harvard in 1988. Through the 1990s he helped found the field of chemical biology, developing diversity-oriented synthesis — methods for building large, structurally diverse small-molecule collections — as a way to probe biology the way genetics probes it with mutations. In 1997 he became founding director of Harvard's Institute of Chemistry and Cell Biology, whose screening infrastructure and chemical-genetics philosophy fed directly into the 2004 founding of the Broad Institute, where he built and led its Chemical Biology Program.

Schreiber is a Howard Hughes Medical Institute Investigator (now Emeritus) and a member of the National Academy of Sciences, the National Academy of Medicine, and the American Academy of Arts and Sciences; he has received the Wolf Prize in Chemistry, among other honors. In 2024 he co-founded Arena BioWorks, a privately funded biomedical research institute in Cambridge, MA, which closed in November 2025.

Milestones in the Atlas

A selection, not a full bibliography: only papers that meet the Atlas inclusion criteria.

YearEvidenceStudy
1994 M A mammalian protein targeted by G1-arresting rapamycin-receptor complex BRO1994 Purifies FRAP (now called mTOR) as the mammalian protein bound by the FKBP12–rapamycin complex, identifying the direct molecular target of rapamycin.
1996 M Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP CHO1996 Solves the crystal structure of FKBP12–rapamycin bound to mTOR's FRB domain, showing rapamycin acts as a molecular glue that plugs into two protein pockets at once.

Co-authors in the Atlas 2

People with a profile here who share at least one study with Stuart L. Schreiber.

ShowHide
  • Eric J. Brown Co-discoverer of mTOR: as first author he isolated the mammalian protein bound by the rapamycin-FKBP12 complex (FRAP) and cloned its gene in 1994.
  • Jon Clardy Chemist who solved the crystal structure of the FKBP12-rapamycin-FRB (mTOR) complex, showing how rapamycin acts as a molecular glue between two proteins.

Every researcher with a profile →

← All researchers

Spotted something wrong or out of date about Stuart L. Schreiber?
Was this page useful?