Hyo J Yang
Researcher in Nikola Pavletich's structural biology laboratory at Memorial Sloan Kettering and co-author of the two Nature papers that showed the atomic structure of mTOR and of mTORC1
Structural Biology Program, Memorial Sloan Kettering Cancer Center (Pavletich laboratory, papers 2013 and 2017; at the time of the studies)
Hyo J Yang is a co-author of two structure papers from Nikola Pavletich's laboratory at Memorial Sloan Kettering Cancer Center that changed how mTOR is pictured. Structural biology works out the exact 3D shape of a protein, atom by atom, which shows how it does its job and how drugs fit into it.
The 2013 paper (YAN2013) solved the crystal structure of the mTOR kinase, the part of the protein that adds phosphate groups to its targets. It showed that the active site sits in a deep, narrow cleft, guarded by a section called the FRB domain that acts like a gatekeeper for incoming target proteins. That explained why rapamycin, which binds the FRB domain together with its partner protein FKBP12, blocks mTOR by limiting access to the cleft, and why cancer-causing mutations cluster where they do. The 2017 paper (YAN2017) used cryo-electron microscopy, which images frozen protein complexes with an electron beam, to show the whole mTORC1 complex. It showed how the small protein RHEB, which signals growth, bends mTORC1 into its active shape, and how the inhibitor PRAS40 blocks it. Both papers describe purified proteins, not cells or animals.
These two papers are the only PubMed records for Yang with Pavletich, and no other publication or institutional page could be firmly tied to this name, which is common. The affiliation shown is the one on the papers. Hyo J Yang is a different person from Haijuan Yang, first author of both papers.
Milestones in the Atlas
A selection, not a full bibliography: only papers that meet the Atlas inclusion criteria.
| Year | Evidence | Study |
|---|---|---|
| 2013 | M | mTOR kinase structure, mechanism and regulation YAN2013 Co-author of the crystal structure of the mTOR kinase, which showed the deep active-site cleft guarded by the FRB domain. |
| 2017 | M | Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40 YAN2017 Co-author of the cryo-EM structures showing how RHEB switches mTORC1 on and how PRAS40 blocks it. |
Co-authors in the Atlas 2
People with a profile here who share at least one study with Hyo J Yang.
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- Haijuan Yang 2 shared studies Solved, as first author in the Pavletich lab, the crystal structure of the mTOR kinase and the structure of mTORC1 activated by RHEB
- Nikola P. Pavletich 2 shared studies Solved the crystal structure of the mTOR kinase, revealing the FRB domain as a gatekeeper of its active site, and later showed how RHEB switches mTORC1 on and PRAS40 blocks it
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