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Mechanistic target of rapamycin complex 2 (mTORC2) is crucial for cell proliferation. Its cryo-EM structure reveals how Rictor and mSin1 inhibit rapamycin binding, explaining mTORC2

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Signaling

Background:

  • Mechanistic target of rapamycin (mTOR) complex 2 (mTORC2) regulates cell proliferation via AGC kinase phosphorylation.
  • mTORC2 comprises mTOR, mLST8, Rictor, and mSin1.

Purpose of the Study:

  • Investigate intermolecular interactions within the mTORC2 complex.
  • Determine the cryo-electron microscopy (cryo-EM) structure of mTORC2.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) at 4.9 Å resolution.
  • Structural analysis of intermolecular interactions.

Main Results:

  • The mTORC2 structure exhibits a hollow rhombohedral fold with 2-fold symmetry.
  • Dimerized mTOR acts as a scaffold; Rictor and mSin1 interact with mTOR, inhibiting rapamycin binding.
  • mTORC2's dimer conformation is more compact than mTORC1's, and Rictor/Raptor binding to mTOR is mutually exclusive.

Conclusions:

  • Provides the structural basis for mTORC2 assembly and rapamycin insensitivity.
  • Offers a framework for understanding mTORC2 pathway regulation.