Eric Spooner
Manager of the Whitehead Institute's Proteomics Core Facility, whose mass spectrometry work identified proteins in complexes for many Whitehead studies, including two on amino acid sensing upstream of mTORC1
Facility manager, Proteomics Core Facility, Whitehead Institute for Biomedical Research (Whitehead profile, 2020; PubMed affiliation through 2024)
Portrait: Conor Gearin / Whitehead Institute
Many discoveries about mTORC1, the growth-control complex, began by pulling one protein out of cells and asking which other proteins came with it. The answer comes from mass spectrometry, which weighs protein fragments and identifies them. Eric Spooner runs that step at the Whitehead Institute, and he is a co-author on two Atlas papers from David Sabatini's lab that relied on it.
In TSU2013, the lab showed that folliculin, a tumour suppressor, works with its partner FNIP as a GAP for the Rag GTPases RagC and RagD; a GAP is a helper that makes a switch protein turn itself off. RagC or RagD in this GDP-bound state is needed for the Rags to bind mTORC1 and bring it to the lysosome when amino acids are present. In CHA2014, the lab found that the Sestrin proteins bind GATOR2 and so damp the amino acid signal to mTORC1. Both were done in cultured cells.
A 2020 Whitehead Institute profile describes Spooner as manager of the Proteomics Core Facility, with more than 20 years of protein analysis behind him, most of it running the core. The facility measures protein levels, maps how complexes are built and studies protein interactions, using labelling methods such as SILAC and iTRAQ, high-resolution mass spectrometry and cross-linking. PubMed lists him at the Whitehead Institute on more than forty papers, the most recent in 2024.
Milestones in the Atlas
A selection, not a full bibliography: only papers that meet the Atlas inclusion criteria.
| Year | Evidence | Study |
|---|---|---|
| 2013 | M | The folliculin tumor suppressor is a GAP for the RagC/D GTPases that signal amino acid levels to mTORC1 TSU2013 Co-author on the cell study showing that folliculin-FNIP is a GAP for RagC and RagD, needed for amino acids to bring mTORC1 to the lysosome. |
| 2014 | M | The Sestrins interact with GATOR2 to negatively regulate the amino-acid-sensing pathway upstream of mTORC1 CHA2014 Co-author on the cell study showing that the Sestrins bind GATOR2 to damp amino acid signalling to mTORC1. |
Co-authors in the Atlas 12
People with a profile here who share at least one study with Eric Spooner.
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- David M. Sabatini 2 shared studies Identified mTOR (as RAFT1) in 1994. His lab then mapped much of the machinery around it: raptor and rictor at the core of mTORC1 and mTORC2, the Rag–Ragulator system that docks mTORC1 on the lysosome, and the sensors that detect leucine, arginine and SAM
- Liron Bar-Peled 2 shared studies Showed as a Sabatini-lab graduate student that Ragulator switches the Rag GTPases on, acting as their GEF. He also discovered GATOR1 and GATOR2; GATOR1 switches the Rags off and its genes are mutated in some cancers
- Lynne Chantranupong 2 shared studies Showed as a Sabatini-lab graduate student that the Sestrins act through GATOR2 to regulate amino-acid signalling to mTORC1. She then discovered the CASTOR proteins, the cell's arginine sensors for the pathway
- Choah Kim Researcher in David Sabatini's lab at the Whitehead Institute who contributed to three studies on how amino acids at the lysosome are sensed by mTORC1
- Jose M. Orozco Researcher trained in David Sabatini's laboratory at the Whitehead Institute and MIT who showed that mTORC1 senses glucose through the glycolysis metabolite DHAP
- Rachel L. Wolfson Identified Sestrin2 as the direct leucine sensor of the mTORC1 pathway as a Sabatini-lab MD-PhD student. She also co-discovered KICSTOR, the complex that recruits GATOR1 to the lysosome
- Robert A. Saxton Solved, as a Sabatini-lab graduate student, the structures of the leucine sensor Sestrin2 and the arginine sensor CASTOR1, showing how each one grips its amino acid. He also co-wrote a widely cited 2017 review of mTOR signalling with David Sabatini
- Roberto Zoncu Showed as a postdoc that mTORC1 senses amino acids from inside the lysosome, through the v-ATPase and Ragulator. His Berkeley lab has since mapped how the Rag GTPases and the folliculin complex switch mTORC1 on, and how lysosomal cholesterol feeds into the same system
- Sonia M. Scaria Contributed, as an MIT undergraduate in the Sabatini lab, to the discovery of CASTOR1 as the arginine sensor and SAMTOR as the SAM sensor of the mTORC1 pathway
- Steven P. Gygi Mass-spectrometry scientist whose Harvard lab builds large-scale proteomics methods, including the BioPlex human protein-interaction map, and contributed proteomics to the discoveries of the CASTOR and SAMTOR nutrient sensors
- Tim Wang Co-developed genome-wide CRISPR screening in human cells (reported in parallel by Feng Zhang's lab) as a graduate student with David Sabatini and Eric Lander, and contributed to studies showing that the 4E-BPs mediate mTORC1's control of translation and that CASTOR1 senses arginine
- Zhi-Yang Tsun Biologist who, as first author in David Sabatini's lab, showed that the tumour suppressor folliculin is a GAP for the RagC and RagD GTPases that carry the amino acid signal to mTORC1
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