Roger L. Williams
Solved structures showing how the Rag GTPases bind mTORC1 and how TOR forms a dimer, working at the MRC Laboratory of Molecular Biology
Group Leader, MRC LMB, Cambridge · Rutgers, Cornell, Boris Kidrič Institute Belgrade · PhD, UC Riverside (1986) · MS, Eastern Washington Univ. · BS, Purdue
MRC Laboratory of Molecular Biology (LMB), Cambridge (Cambridge, England, United Kingdom) ↗ ORCID0000-0001-7754-4207 ↗
Portrait: MRC Laboratory of Molecular Biology (LMB), Cambridge
Cryo-EM shows TOR dimerizes through an N-terminal helical solenoid (BAR2016), shaping how mTORC1 is built. Three years later, solved mTORC1 bound to Rag GTPases (ANA2019), showing how amino-acid status recruits the complex to the lysosome.
Leads a structural biology group at the storied MRC LMB, working across the PI3K superfamily. FRS (2017), FMedSci, EMBO Member, Biochemical Society Morton Lectureship.
Milestones in the Atlas
A selection, not a full bibliography: only papers that meet the Atlas inclusion criteria.
| Year | Evidence | Study |
|---|---|---|
| 2016 | M | Tor forms a dimer through an N-terminal helical solenoid with a complex topology BAR2016 Cryo-EM shows TOR dimerizes through an N-terminal helical solenoid. |
| 2019 | M | Architecture of human Rag GTPase heterodimers and their complex with mTORC1 ANA2019 Structures of Rag GTPase heterodimers bound to mTORC1 reveal lysosomal recruitment mechanism. |
Co-authors in the Atlas 6
People with a profile here who share at least one study with Roger L. Williams.
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- Alex Berndt 2 shared studies Protein scientist in Roger Williams' group at the MRC Laboratory of Molecular Biology who helped solve structures of PI3K enzymes and of mTOR and its partners
- Christopher Johnson 2 shared studies Biophysicist who built and ran the Biophysics Facility at the MRC Laboratory of Molecular Biology, measuring how proteins fold, bind and change shape for dozens of research groups
- 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
- Domagoj Baretić Structural biologist who, while at the MRC Laboratory of Molecular Biology, solved early cryo-EM structures of Tor and its relatives, and now works on ADP-ribosylation enzymes at Oxford
- Kacper B. Rogala Solved the near-atomic cryo-EM structure that shows how mTORC1 physically docks at the lysosome by reading the Rag GTPases
- Madhanagopal Anandapadamanaban Structural biologist at the MRC Laboratory of Molecular Biology who solved the structure of the human Rag GTPases bound to mTORC1, showing how amino acids bring mTORC1 to the lysosome
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