Eunjung Kim
Showed as first author, in Kun-Liang Guan's lab, that the Rag GTPases relay amino-acid availability to TORC1, in parallel with the Sabatini lab's discovery
Postdoctoral researcher, Kun-Liang Guan lab, UCSD (circa 2007–2010) · first author, landmark 2008 Rag GTPase discovery · later career not reliably traceable
Before 2008, scientists knew amino acids switch on mTORC1 but not how that signal physically reached the enzyme. In 2008, two labs independently reported the answer: Yasemin Sancak in David Sabatini's lab (Science) and Eunjung Kim in Kun-Liang Guan's lab (Nature Cell Biology) both showed that the Rag GTPases are needed for amino acids to switch on mTORC1. The Sabatini paper also showed that the Rags bind raptor and move mTORC1 to the compartment that holds its activator Rheb; that this is the lysosome surface was established by the same lab in 2010. Kim was first author on the Guan lab's paper, built largely on Drosophila genetics and mammalian cell experiments — now textbook mTOR biology.
Kim appears as a co-author on two other Guan-lab papers from the same period, indicating she continued in the lab for at least a couple more years. Her subsequent career could not be reliably traced — 'Eunjung Kim' is a very common Korean name and no confidently-matched later publication record was found.
Milestones in the Atlas
| Year | Evidence | Study |
|---|---|---|
| 2008 | M | Regulation of TORC1 by Rag GTPases in nutrient response KIM2008 First author on the 2008 discovery that Rag GTPases activate TORC1 in response to amino acids — one of two simultaneous, independent 2008 papers that established the amino-acid-sensing arm of the mTOR pathway. |
Co-authors in the Atlas
People with a profile here who share at least one study with Eunjung Kim.
- Kun-Liang Guan Showed how growth-factor and energy signals reach mTORC1 through TSC2 and Rheb, and, in parallel with the Sabatini lab, that the Rag GTPases carry the amino-acid signal. His lab also found that AMPK and mTORC1 control autophagy by phosphorylating the kinase ULK1 at different sites