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
Roger Williams group, MRC Laboratory of Molecular Biology, Cambridge (papers 2010–2021; at the time of the studies)
Portrait: LinkedIn
Alex Berndt is a co-author of two structural papers in the Atlas from Roger Williams' group at the MRC Laboratory of Molecular Biology. The first (BAR2016) used cryo-electron microscopy on the Tor kinase bound to its partner Lst8. It showed that Tor pairs up into a dimer through a long, coiled stretch of helices at its front end, which helped explain how the much larger mTORC1 complex is built. The second (ANA2019) solved structures of the human Rag GTPases, the switch proteins that dock mTORC1 on the lysosome when amino acids are present, and showed how they bind mTORC1.
Berndt's work in the Williams group goes back to 2010, when Berndt was first author of a Nature Chemical Biology paper on the structure of p110delta, a PI3K enzyme important in immune cells, which showed how new inhibitors fit into it. PI3K and mTOR are related kinases with similar active sites. Berndt also contributed to a 2011 paper on how PI3K enzymes are switched on at membranes and to a 2021 eLife study on how the inhibitor protein DEPTOR binds mTOR.
No current institutional page could be confirmed, so the affiliation shown is the one on the Atlas papers.
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 Co-author of the cryo-EM study showing that Tor forms a dimer through a long helical region at its N-terminus. |
| 2019 | M | Architecture of human Rag GTPase heterodimers and their complex with mTORC1 ANA2019 Co-author of the structural study of the human Rag GTPases and their complex with mTORC1. |
Co-authors in the Atlas 6
People with a profile here who share at least one study with Alex Berndt.
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- 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
- Roger L. Williams 2 shared studies Solved structures showing how the Rag GTPases bind mTORC1 and how TOR forms a dimer, working at the MRC Laboratory of Molecular Biology
- 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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