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

Tamir Gonen lab, Howard Hughes Medical Institute, University of California, Los Angeles (papers 2020–2023) · Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, Virginia (papers 2018–2019)

Hsiang-Ting Lei is first author of LEI2018, the crystal structure of SLC38A9 from zebrafish with an arginine molecule bound. SLC38A9 is a transporter in the lysosome membrane that also acts as a sensor: when arginine builds up inside the lysosome, SLC38A9 helps tell mTORC1, the growth-control complex, that amino acids are plentiful. The structure, caught in a state open toward the cytosol, shows exactly where arginine sits and which parts of the protein grip it, giving a physical basis for arginine sensing.

In a 2020 follow-up in the journal Structure, again as first author, Lei solved a second SLC38A9 structure in which the protein's own N-terminal tail is inserted deep into the pocket where arginine normally binds. The team proposed a ball-and-chain model: when arginine is scarce the tail plugs the transporter, and when arginine is abundant the tail is pushed out and becomes free to activate the Rag GTPases and mTORC1.

Lei worked with Tamir Gonen, first at the Janelia Research Campus of the Howard Hughes Medical Institute in Ashburn, Virginia, where the lab also solved structures of an alanine transporter (2019), and then at HHMI at the University of California, Los Angeles, where Lei contributed to cryo-EM structures of the omega-3 fatty acid transporter Mfsd2a (2023). Later positions could not be confirmed.

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