Oliver's mTOR Atlas Evidence Platform
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Tamir Gonen

Determines the 3D structures of membrane proteins and pioneered microcrystal electron diffraction (MicroED); in the mTOR field he solved the structure of the lysosomal arginine transporter SLC38A9.

Professor, Biological Chemistry and Physiology, UCLA · HHMI Investigator (2017) · PhD, University of Auckland (2002)

Gonen Lab, Departments of Biological Chemistry and Physiology, David Geffen School of Medicine, University of California, Los Angeles (Los Angeles, California, USA) ↗

Tamir Gonen Portrait: UCLA

Tamir Gonen is a structural biologist and professor at UCLA, and an Investigator of the Howard Hughes Medical Institute. He studied at the University of Auckland, did structural biology training at Harvard Medical School and later led a group at HHMI's Janelia Research Campus before moving to UCLA.

The Atlas includes his 2018 study of SLC38A9, a protein in the lysosome membrane that moves amino acids and helps mTORC1 sense them. His team used X-ray crystallography on the zebrafish version of the protein with arginine bound.

The structure caught the transporter in a cytosol-open state and showed how a conserved stretch in its first helix holds arginine in place. Changing that stretch stopped arginine transport. This gave a molecular picture of how a lysosomal transporter could report amino acid levels to mTORC1.

Milestones in the Atlas

A selection, not a full bibliography: only papers that meet the Atlas inclusion criteria.

YearEvidenceStudy
2018 M Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state LEI2018 Solved the crystal structure of arginine-bound SLC38A9 from zebrafish, showing how the transporter grips arginine; Gonen was senior and corresponding author.

Co-authors in the Atlas 1

People with a profile here who share at least one study with Tamir Gonen.

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  • Hsiang-Ting Lei Structural biologist from Tamir Gonen's lab who solved crystal structures of the lysosomal arginine sensor SLC38A9, showing how it holds arginine and how its own tail plugs the binding pocket

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