Oliver's mTOR Atlas Evidence Platform
Reading level
Mode

Shuyu Wang

Co-discovered SLC38A9, the lysosomal transporter that senses arginine for mTORC1

MD–PhD, Harvard/MIT MD-PhD Program (2018; PhD in Biology, MIT, thesis “Studies of amino acid sensing by the mTORC1 pathway”, David Sabatini lab, Whitehead Institute) · now postdoctoral fellow, UCSF Department of Psychiatry and Behavioral Sciences (Manoli Lab)

Manoli Lab, UCSF ↗

Shuyu Wang Portrait: UCSF Dept. of Psychiatry and Behavioral Sciences

Shuyu Wang was part of David Sabatini's lab at the Whitehead Institute during the effort to work out exactly how amino acids are sensed inside the lysosome, the organelle where mTORC1 sits when nutrients are plentiful.

In 2011 she was among the authors of the paper showing that lysosomal amino acids activate mTORC1 through an “inside-out” mechanism — the Ragulator/Rag GTPase machinery reads the amino-acid concentration inside the lysosome and, in response, recruits mTORC1 to the lysosomal surface. That paper established that the lysosome itself, not just the cytoplasm, is where mTORC1's nutrient sensing happens.

She then led the 2015 paper that identified the missing piece of that inside-out mechanism: SLC38A9, a lysosomal membrane transporter that physically senses arginine inside the lysosome and signals its sufficiency to mTORC1. SLC38A9 turned out to be a direct physical link between the raw presence of an amino acid and the Rag GTPase switch that turns mTORC1 on.

Wang did this work as an MD–PhD student in the Harvard/MIT program; her MIT thesis (2018) was titled “Studies of amino acid sensing by the mTORC1 pathway.” She then trained in psychiatry at UCSF and is now a postdoctoral research fellow there in Devanand Manoli's lab, studying the neural circuits of social behaviour — a long way from the lysosome, but the SLC38A9 paper remains one of the defining results in nutrient sensing (sources: Harvard/MIT MD-PhD alumni listing; UCSF Psychiatry).

Milestones in the Atlas

YearEvidenceStudy
2011 M mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase ZON2011 Shows lysosomal amino acids activate mTORC1 through an inside-out mechanism, establishing the lysosome as the site of nutrient sensing.
2015 M Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1 WAN2015 Identifies SLC38A9 as the lysosomal transporter that senses arginine and signals its sufficiency directly to mTORC1.

← All researchers