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A toroid is a closely wound donut-shaped coil constructed using a single  conducting wire. In general, it is assumed that a toriod consists of  multiple circular loops perpendicular to its axis.
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The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
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EGOC inhibits TOROID polymerization by structurally activating TORC1.

Manoël Prouteau1, Clélia Bourgoint2, Jan Felix3,4

  • 1Department of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland. manoel.prouteau@unige.ch.

Nature Structural & Molecular Biology
|January 26, 2023
PubMed
Summary
This summary is machine-generated.

Glucose depletion causes yeast Target of rapamycin complex 1 (TORC1) to form inactive TOROID structures. EGO complex (EGOC) activity controls this TORC1 redistribution, revealing a key mechanism for cellular regulation.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Target of rapamycin complex 1 (TORC1) is a crucial protein kinase regulating cell growth and homeostasis.
  • In yeast, glucose deprivation induces TORC1 to form inactive TOROID condensates on the vacuole surface.
  • The precise molecular mechanisms driving TORC1 redistribution remain largely unknown.

Purpose of the Study:

  • To elucidate the mechanisms controlling TORC1 redistribution into TOROID structures upon glucose depletion.
  • To investigate the role of the EGO complex (EGOC) in regulating TORC1 localization and activity.
  • To determine the structural basis of TORC1-TORC1 and TORC1-EGOC interactions within TOROID condensates.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine the structure of TORC1 within TOROIDs.
  • In vivo experiments to interrogate key protein-protein interactions.
  • Manipulation of EGO complex (EGOC) activity to assess its impact on TORC1 localization.

Main Results:

  • Acute modulation of EGO complex (EGOC) activity directly controls TOROID formation and distribution, independent of other nutrient pathways.
  • The 3.9-Å cryo-EM structure reveals TORC1-TORC1 and TORC1-EGOC interaction interfaces.
  • Glucose-dependent EGOC activation binds TORC1, preventing polymerization and promoting the release of active TORC1.

Conclusions:

  • EGO complex (EGOC) plays a pivotal role in glucose-mediated regulation of TORC1 localization and activity.
  • Structural insights reveal how EGOC binding to TORC1 prevents TOROID assembly and facilitates active TORC1 release.
  • This mechanism provides a direct link between nutrient sensing and TORC1 signaling dynamics.