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Toroids01:27

Toroids

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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.
When connected to a supply, the magnetic field generated in the toroid has field lines circular and concentric to its axis. Conventionally, the direction of this magnetic field is expressed using the right-hand rule. If the fingers of the right hand curl in the current direction, the thumb...
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Torque On A Current Loop In A Magnetic Field01:13

Torque On A Current Loop In A Magnetic Field

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The most common application of magnetic force on current-carrying wires is in electric motors. These consist of loops of wire, which are placed between the magnets with a magnetic field. When current flows through the loops, the magnetic field applies torque, which causes the shaft to rotate, thus converting electrical energy to mechanical energy.
Consider a rectangular current-carrying loop containing N turns of wire, placed in a uniform magnetic field. The net force on a current-carrying loop...
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Inhibition of Cdk Activity02:34

Inhibition of Cdk Activity

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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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Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
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Actin Polymerization01:42

Actin Polymerization

6.8K
Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶  nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight...
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Cationic Chain-Growth Polymerization: Mechanism00:57

Cationic Chain-Growth Polymerization: Mechanism

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The cationic polymerization mechanism consists of three steps: initiation, propagation, and termination. In the initiation step of the polymerization process, the π bond of a monomer gets protonated by the Lewis acid catalyst, which is formed from boron trifluoride and water. The protonation of the π bond generates a carbocation stabilized by the electron‐donating group. In the propagation step, the π bond of the second monomer acts as a nucleophile and attacks the...
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Related Experiment Video

Updated: Aug 12, 2025

Author Spotlight: Unveiling the Role of TMOD3 in Platinum Resistance and Immune Infiltration in Ovarian Cancer
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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.