Hediye Erdjument-Bromage
Ran the proteomics that put names to the unknown bands in the raptor and rictor purifications
Proteomics & mass spectrometry · Memorial Sloan Kettering Cancer Center → NYU Langone Health Mass Spectrometry Core for Neuroscience
Mass Spectrometry Core, NYU Langone ↗
Hediye Erdjument-Bromage is a biochemist whose postdoctoral training introduced her to mass spectrometry and proteomics, a technical specialty she has practiced ever since. For many years she managed the microchemistry and proteomics core laboratory at Memorial Sloan Kettering Cancer Center, before moving to NYU Langone Health, where she now co-runs the Mass Spectrometry Core for Neuroscience.
Her core facility's protein-identification work was essential to the biochemical purification papers that discovered raptor and rictor — identifying, from tiny amounts of co-purified material, the specific proteins bound to mTOR that turned out to define its two distinct complexes. That kind of unbiased mass-spectrometry identification underlies much of the molecular parts-list this Atlas documents.
The studies below, gathered in this Atlas, mark her contribution.
Milestones in the Atlas
| Year | Evidence | Study |
|---|---|---|
| 2002 | M | mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery KIM2002 Mass-spectrometry identification of raptor, the defining subunit of mTORC1. |
| 2003 | M | GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR KIM2003 Discovered mLST8 (GbetaL), the third core subunit that clamps onto mTOR's kinase domain and stabilizes the complex. It fine-tunes how tightly Raptor holds mTOR in response to nutrients - a small but essential cog that later turned out to be especially critical for the mTORC2 complex. |
| 2004 | M | Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton SAR2004 Mass-spectrometry identification of rictor, the defining subunit of mTORC2. |
| 2005 | M | Phosphorylation and functional inactivation of TSC2 by Erk implications for tuberous sclerosis and cancer pathogenesis MA2005 Contributes proteomics analysis to the identification of TSC2 phosphorylation by Erk. |