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Electrostatic Boundary Conditions01:16

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Micro-drive Array for Chronic in vivo Recording: Tetrode Assembly
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Electrostatic lateral interactions drive ESCRT-III heteropolymer assembly.

Sudeep Banjade1,2, Shaogeng Tang1,2, Yousuf H Shah1,2

  • 1Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.

Elife
|June 28, 2019
PubMed
Summary

The ESCRT-III complex, crucial for cell processes, forms flexible structures via subunit interactions. This study reveals electrostatic interactions between Snf7 and Vps24 subunits drive ESCRT-III polymer assembly and flexibility.

Keywords:
ESCRT-IIIS. cerevisiaeSnf7Vps24biochemistrycell biologychemical biologymultivesicular bodiespolymersself-assembly

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The Endosomal Sorting Complexes Required for Transport (ESCRT)-III complex is essential for various cellular membrane remodeling events.
  • ESCRT-III subunits form hetero-polymers with diverse architectures, but the precise mechanisms governing inter-subunit recognition and flexibility remain incompletely understood.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying the specific recruitment of ESCRT-III subunits and the formation of flexible hetero-polymer architectures.
  • To investigate the role of electrostatic interactions in mediating the assembly and functional dynamics of the ESCRT-III complex.

Main Methods:

  • In vivo and in vitro biochemical assays were employed to study the interactions between ESCRT-III subunits.
  • Site-directed mutagenesis, specifically charge-inversion mutations in the conserved acidic helix of Snf7, was used to probe the role of electrostatic interactions.
  • Functional assays were performed to assess the impact of mutations on Snf7-Vps24 interactions and polymer assembly.

Main Results:

  • The Saccharomyces cerevisiae ESCRT-III subunit Snf7 utilizes a conserved acidic helix to recruit its partner Vps24.
  • Charge-inversion mutations within this helix disrupt lateral Snf7-Vps24 interactions, while charge rebalancing rescues these defects, indicating a crucial role for electrostatics.
  • These findings support a model where cooperative electrostatic interactions drive specific inter-subunit recognition and enable polymer flexibility through lateral sliding.

Conclusions:

  • ESCRT-III hetero-polymer assembly is governed by electrostatic interactions, rather than strict residue-to-residue specificity, allowing for adaptable polymer architectures.
  • A model is proposed where cooperative electrostatic forces facilitate specific subunit recognition, and polymer sliding accommodates dynamic changes in structure during membrane remodeling.
  • This study reveals a mechanism coupling interaction specificity with polymer flexibility in membrane-remodeling heteropolymeric assemblies.