Sunghoon Kim
Senior author of the 2012 study proposing leucyl-tRNA synthetase as an intracellular leucine sensor for mTORC1, part of his broader work on the signalling roles of tRNA synthetases
Biochemist · Yonsei University (since 2020; Seoul National University 2001–2020) – known for work on the "moonlighting" signaling roles of tRNA synthetases · Ho-Am Prize laureate
Sunghoon Kim is one of the most decorated biochemists in South Korea. He is the senior/corresponding author of Han JM et al., Cell 2012, which proposed an answer to a long-standing puzzle: how cells directly sense intracellular leucine levels to switch on mTORC1. His group showed that leucyl-tRNA synthetase (LRS) — an enzyme whose textbook job is attaching leucine to its tRNA for protein synthesis — moonlights as a leucine sensor, binding the Rag GTPase in a leucine-dependent manner and acting as a GAP toward RagD. The model remains debated: Sestrin2 (2015) is now the best-supported leucine sensor upstream of mTORC1.
That discovery sits inside a decades-long research program: PhD at Brown University (1991), postdoctoral work at MIT, and a career at Seoul National University (2001–2020) and, since 2020, Yonsei University, directing a sequence of national research centers on aminoacyl-tRNA synthetases — most recently the Medicinal Bioconvergence Research Center. His lab found that several components of the multi-tRNA synthetase complex, notably the associated proteins AIMP2 and AIMP3, act as tumor suppressors, part of a wider body of work by several groups showing that tRNA synthetases also act as signaling molecules in human disease. He has received Korea's Top Scientist and Technologist Award (2006), the Korean National Academy of Science Award (2012), and the Ho-Am Prize in Medicine (2015) — often described as Korea's answer to the Nobel Prize.
Milestones in the Atlas
| Year | Evidence | Study |
|---|---|---|
| 2012 | M | Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway HAN2012 Senior/corresponding author proposing leucyl-tRNA synthetase as an intracellular leucine sensor that activates mTORC1, a model that competes with the Sestrin2 model and remains debated. |