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A corkscrew model for dynamin constriction.

Jason A Mears1, Pampa Ray, Jenny E Hinshaw

  • 1Laboratory of Cell Biochemistry and Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, 8 Center Drive, MSC 0851, Bethesda, MD 20892, USA.

Structure (London, England : 1993)
|October 17, 2007
PubMed
Summary
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Dynamin, a GTPase protein, constricts cell membranes through a corkscrew-like motion. This study reveals dynamin

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Structural Biology

Background:

  • The protein dynamin is crucial for various membrane vesiculation processes in eukaryotic cells.
  • Dynamin functions as a large GTPase, mediating the constriction of lipid bilayers.

Purpose of the Study:

  • To develop a coherent structural model of dynamin-mediated membrane constriction.
  • To elucidate the molecular mechanisms underlying dynamin's role in membrane dynamics.

Main Methods:

  • Integration of X-ray crystallography and cryo-electron microscopy (cryo-EM) data.
  • Fitting of dynamin domains (GTPase, Middle, GTPase Effector, Pleckstrin Homology) to cryo-EM structures.
  • Proteolysis and immunogold labeling experiments to confirm domain topology.

Related Experiment Videos

Main Results:

  • A structural model of dynamin bound to lipid bilayers in both nonconstricted and constricted states was generated.
  • Confirmation of dynamin domain topology within helical arrays.
  • Identification of a twisting motion in dynamin domains correlating with conformational changes observed via cryo-EM.

Conclusions:

  • A corkscrew model for dynamin-mediated membrane constriction is proposed.
  • Key sequence regions important for dynamin function are predicted for future studies.