Three-step docking by WIPI2, ATG16L1 and ATG3 delivers LC3 to the phagophore: Molecular dynamics simulation dat

By Shanlin Rao, PhD and Gerhard Hummer, PhD
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Output Details

Description
Atomistic molecular dynamics simulation data set accompanying manuscript 10.1101/2023.07.17.549391.
Identifier (DOI)
10.5281/zenodo.8083723
Tags
  • ATG12-5-16L1
  • ATG3 (E2-like enzyme)
  • In Silico
  • LC3 lipidation
  • Molecular Dynamics simulation (MD)
Team
Team Hurley
Program
Collaborative Research Network
Theme
PD Functional Genomics

Meet the Authors

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    Shanlin Rao, PhD

    Key Personnel: Team Hurley, 

    Max Planck Institute of Biophysics

  • Gerhard Hummer, PhD

    Collaborating PI: Team Hurley, 

    Max Planck Institute of Biophysics

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Three-step docking by WIPI2, ATG16L1 and ATG3 delivers LC3 to the phagophore

In this manuscript, in a near-complete pathway from initial membrane recruitment to LC3 lipidation reaction, we show how a three-step targeting mechanism of the ATG12-ATG5-ATG16L1 machinery ensures a high level of regulatory control on autophagy.

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Membrane tube assay data for Jensen et al, 2022

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Membrane curvature sensing and stabilization by the autophagic LC3 lipidation machinery

During autophagy initiation, the curved phagophore is stabilized. Using in vitro reconstitution and MD simulations, authors show that WIPI2 and ATG16L1 bind these curved phagophores and the ATG12-5-16L1 complex is responsible for membrane curvature.

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