Roger L. Williams
Reveals the atomic architecture that docks mTORC1 onto the lysosome
BS, Purdue · MS, Eastern Washington Univ. · PhD, UC Riverside (1986) · Rutgers, Cornell, Boris Kidrič Institute Belgrade · Group Leader, MRC LMB, Cambridge
MRC Laboratory of Molecular Biology (LMB), Cambridge ↗
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
| 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. |