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A Phosphate Tag Flips the Cell's Growth Switch
Structural work shows how one enzyme can switch between amino-acid sensing and mTORC1 activation through a reversible modification.
Summary
Structural work shows how one enzyme can switch between amino-acid sensing and mTORC1 activation through a reversible modification.
A KAIST team reports that methionyl-tRNA synthetase, or MARS1, responds to amino acids by releasing LARS1 and changing phosphorylation state, which lets LARS1 help activate the mTORC1 growth pathway. Structural and cell experiments trace how the same protein can alternate between its translation role and growth signaling. The mechanism offers a potential drug target, but this is basic molecular work rather than evidence of a cancer therapy.
Why it matters
Structural work shows how one enzyme can switch between amino-acid sensing and mTORC1 activation through a reversible modification.
Limits and context
No additional limitation was separately recorded.
Key claims
Structural work shows how one enzyme can switch between amino-acid sensing and mTORC1 activation through a reversible modification.
Evidence: source-2026-07-26-006
Sources
- KAIST via EurekAlert: Molecular switch for mTORC1 growth signalingKAIST via EurekAlert · secondary reporting
Corrections
No corrections have been recorded for this story.