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Regulation of the Unfolded Protein Response

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Structural basis for ESCRT-III protein autoinhibition.

Monika Bajorek1, Heidi L Schubert, John McCullough

  • 1Department of Biochemistry, University of Utah, Salt Lake City, Utah, USA.

Nature Structural & Molecular Biology
|June 16, 2009
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Increased sodium tolerance-1 (IST1) is a new member of the ESCRT-III protein family. Its interaction with CHMP1B is crucial for cell abscission, and alpha5 helix dissociation activates ESCRT-III assembly.

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13:57

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Published on: February 18, 2014

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

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09:16

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Published on: March 25, 2020

Area of Science:

  • Cell biology
  • Molecular biology
  • Structural biology

Background:

  • Endosomal sorting complexes required for transport-III (ESCRT-III) proteins regulate membrane dynamics.
  • ESCRT-III subunits cycle between soluble monomers and membrane-bound assemblies.
  • These complexes are vital for processes like vesicle formation, cell division, and viral budding.

Purpose of the Study:

  • To investigate the structural and functional relationship of IST1 within the ESCRT-III machinery.
  • To elucidate the mechanism of ESCRT-III activation and assembly.

Main Methods:

  • X-ray crystallography to determine the structures of IST1 and CHMP3 core domains.
  • In vitro assembly assays to study protein polymerization.
  • Analysis of IST1-CHMP1B interactions and their role in abscission.
  • Mutational analysis of the CHMP3 core-alpha5 interface.

Main Results:

  • IST1 shares structural homology with ESCRT-III proteins, identifying it as a new member.
  • IST1 and CHMP1B form higher-order helical structures in vitro.
  • IST1-CHMP1B interactions are essential for midbody abscission.
  • The alpha5 helix of CHMP3 can autoinhibit core domain assembly.
  • Mutations disrupting the CHMP3 core-alpha5 interface enhance assembly and HIV inhibition.

Conclusions:

  • IST1 is a functional ESCRT-III component involved in abscission.
  • The autoinhibitory role of the alpha5 helix is a conserved mechanism for ESCRT-III activation.
  • Dissociation of the alpha5 helix from the core domain is critical for ESCRT-III assembly at membranes.