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
Sir William Dunn School of Pathology, University of Oxford (papers since 2024) · MRC Laboratory of Molecular Biology, Cambridge (Roger Williams group, then Joseph Yeeles group, papers 2014–2020)
mTOR is a huge protein, and for years nobody knew what its long front section looked like. Domagoj Baretić's 2016 paper in Nature Communications (BAR2016), from Roger Williams' group at the MRC Laboratory of Molecular Biology in Cambridge, used cryo-electron microscopy, a method that images frozen protein particles and combines thousands of pictures into a 3D model. Working with Tor bound to its partner protein Lst8, the team found that Tor pairs up into a dimer, and that its N-terminal region forms a long solenoid of stacked helices with an unusually complex fold. This helped explain the overall shape of mTORC1, which is also built as a dimer.
Baretić had earlier co-written a 2014 review with Williams on the structural basis of mTOR function, and in 2019 was first author of a review on the related DNA-damage sensors DNA-PKcs, ATM and ATR, which share mTOR's kinase design. A 2020 Molecular Cell paper, from Joseph Yeeles' group at the LMB, then showed by cryo-EM how the fork protection complex sits on the DNA replication machinery.
Since 2024 Baretić has published from the Sir William Dunn School of Pathology at the University of Oxford, in structural work with Ivan Ahel's and Marcin Suskiewicz's groups on enzymes that attach ADP-ribose to proteins. This includes a 2025 Nature Structural and Molecular Biology paper, as first author, on filament formation by the unusual human sirtuins FAM118, and contributions on PARP enzymes in the interferon response and in cancer drug action.
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 First author: solved the cryo-EM structure showing that Tor dimerizes through a long N-terminal helical solenoid. |
Co-authors in the Atlas 3
People with a profile here who share at least one study with Domagoj Baretić.
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- Alex Berndt 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 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
- 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
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