Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway

@article{Saxton2016StructuralBF,
  title={Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway},
  author={Robert A Saxton and Kevin E. Knockenhauer and Rachel L. Wolfson and Lynne Chantranupong and Michael E Pacold and Tim Wang and Thomas U Schwartz and David M. Sabatini},
  journal={Science},
  year={2016},
  volume={351},
  pages={53-58}
}
Eukaryotic cells coordinate growth with the availability of nutrients through the mechanistic target of rapamycin complex 1 (mTORC1), a master growth regulator. Leucine is of particular importance and activates mTORC1 via the Rag guanosine triphosphatases and their regulators GATOR1 and GATOR2. Sestrin2 interacts with GATOR2 and is a leucine sensor. Here we present the 2.7 angstrom crystal structure of Sestrin2 in complex with leucine. Leucine binds through a single pocket that coordinates its… CONTINUE READING

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