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GTP hydrolysis triggers membrane remodeling by AMPH-1.

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  • 1Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77845, USA.

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Amphiphysin protein AMPH-1 drives transport carrier formation by binding and hydrolyzing guanine nucleotides. This process involves membrane tubulation and lattice formation, crucial for returning molecules to the cell surface.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Membrane Trafficking

Background:

  • Membrane-enclosed transport carriers mediate molecular return from recycling endosomes to the plasma membrane.
  • The precise mechanism of carrier formation remains incompletely understood.
  • In Caenorhabditis elegans, amphiphysin (AMPH-1) is essential for carrier biogenesis from recycling endosomes.

Purpose of the Study:

  • To elucidate the molecular mechanism by which AMPH-1 facilitates transport carrier formation.
  • To propose and test a model linking guanine nucleotide binding and hydrolysis to AMPH-1's membrane remodeling functions.
  • To understand the role of AMPH-1's structural dynamics in membrane tubulation and vesiculation.

Main Methods:

  • Biochemical assays using purified AMPH-1 and liposomes.
  • Investigation of AMPH-1's interaction with membranes in different guanine nucleotide-bound states (GTP vs. GDP).
  • Structural analysis of AMPH-1's role in membrane tubulation and oligomerization.

Main Results:

  • Purified AMPH-1 alone can induce tubulation and vesiculation of liposomes.
  • Guanine nucleotide binding regulates AMPH-1's membrane association and structural transitions.
  • GTP binding stabilizes AMPH-1-membrane interactions via N-terminal amphipathic helices.
  • GDP-bound AMPH-1 forms an oligomeric lattice that tubulates membranes, preceding fission.

Conclusions:

  • A model is proposed where GTP binding and hydrolysis drive AMPH-1-mediated membrane remodeling for carrier formation.
  • AMPH-1's conformational changes, regulated by guanine nucleotides, are critical for organizing membrane structures necessary for transport.
  • This study provides mechanistic insights into the role of amphiphysins in endosomal recycling and membrane trafficking.