Timm Maier
Solved some of the first cryo-EM structures of human mTORC1 (with Nenad Ban's group) and mTORC2, including a high-resolution map of mTORC2
Full professor of Structural Biology, Biozentrum (2023) · associate professor, Biozentrum (2016) · assistant professor, Biozentrum (2011) · postdoc, ETH Zurich (Nenad Ban) · PhD, Freie Universität Berlin (Wolfram Saenger)
Maier Lab, Biozentrum, University of Basel (Basel, Switzerland) ↗ Lab lineagetrained under Nenad Ban → Bluesky@maier-lab.bsky.social ↗ ORCID0000-0002-7459-1363 ↗
Portrait: University of Basel, Biozentrum
With Nenad Ban's group, produced one of the first cryo-EM structures of complete human mTORC1 (AYL2015, 5.9 Å), revealing its rigid dimeric assembly. Five years later, solved mTORC2 at 3.2 Å (SCA2020), pinpointing Rictor's C-terminal tail as the reason mTORC2 isn't directly blocked by rapamycin.
Trained under crystallographer Saenger, then structural biologist Nenad Ban. Continues combining cryo-EM, X-ray, and computation to map large regulatory complexes at atomic resolution.
Milestones in the Atlas
A selection, not a full bibliography: only papers that meet the Atlas inclusion criteria.
| Year | Evidence | Study |
|---|---|---|
| 2015 | M | Architecture of human mTOR complex 1 AYL2015 One of the first cryo-EM structures of complete human mTORC1, revealing dimeric architecture and active-site access. |
| 2018 | M | Architecture of the human mTORC2 core complex STU2018 Architecture of the human mTORC2 core complex (mTOR-Rictor-SIN1-mLST8). |
| 2020 | M | The 3.2-Å resolution structure of human mTORC2. SCA2020 Cryo-EM structure of human mTORC2 pinpoints Rictor's C-terminus as source of rapamycin insensitivity. |
| 2022 | R | mTOR substrate phosphorylation in growth control BAT2022 Review cataloguing direct mTOR substrates and how mTORC1/2 achieve substrate specificity. |
Co-authors in the Atlas 10
People with a profile here who share at least one study with Timm Maier.
ShowHide
- Michael N. Hall 4 shared studies Discovered TOR in yeast in 1991 and established it as a central controller of cell growth that responds to nutrients. His lab later showed that TOR works in two distinct complexes, TORC1 and TORC2, only one of which is blocked by rapamycin
- Daniel Boehringer 3 shared studies Electron microscopy specialist at ETH Zurich whose cryo-EM work underpins the Atlas structures of human mTORC1 and mTORC2
- Nenad Ban 3 shared studies Structural biologist known for atomic structures of the ribosome and for work on how cells make, fold and sort proteins.
- Stefan Imseng 3 shared studies Structural biologist from Timm Maier's group at the Biozentrum Basel who helped solve the first detailed structures of human mTORC1 and mTORC2 and then worked on a drug to block mTORC1 specifically
- Alain Scaiola 2 shared studies Structural biologist in Nenad Ban's group at ETH Zurich who solved the 3.2-angstrom cryo-EM structure of human mTORC2 and works on how ribosomes are built and how new proteins are processed
- Edward Stuttfeld 2 shared studies Structural biologist who led the 2018 eLife study that gave the first detailed picture of the human mTORC2 core complex, working in Timm Maier's lab in Basel
- Evelyn Sauer 2 shared studies Structural biologist at the Biozentrum Basel who worked on the structure of the mTOR kinase and contributed to the cryo-EM structures of human mTORC1 and mTORC2
- Christopher Aylett 2 shared studies Structural biologist who solved the first cryo-EM architecture of human mTORC1 at ETH Zurich and now leads a cryo-EM group at Imperial College London
- Mitsugu Shimobayashi Metabolism researcher who trained with Michael Hall in Basel on mTOR in fat tissue and now leads a group at KU Leuven studying how fat and liver control sugar and lipid storage
- Stefania Battaglioni Cell biologist in Michael Hall's group at the Biozentrum Basel, first author of a 2022 Cell review that catalogued the direct substrates of mTOR
Every researcher with a profile →
Thank you. That helps us know which pages have been read by someone who knows the work.
Thank you. We will check it and correct the page.
Thank you. Your answer was counted anonymously.