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Updated: Sep 9, 2025

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Conformational Rearrangement of Fission DSPs.

Anelise N Hutson1, Kristy Rochon2, Jason A Mears1,3,4

  • 1Department of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.

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Summary
This summary is machine-generated.

Dynamin superfamily proteins (DSPs) like dynamin and Drp1 are key to membrane remodeling. This review details their structural changes and regulation during membrane constriction for organelle dynamics and disease therapies.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Dynamin superfamily proteins (DSPs) are large GTPases essential for membrane remodeling processes.
  • Key DSPs, dynamin and dynamin-related protein 1 (Drp1), share structural similarities but have distinct functions in vesicle trafficking and organelle fission.

Purpose of the Study:

  • To review the conformational changes of mammalian fission DSPs, dynamin and Drp1.
  • To elucidate the structural basis of DSP activation, self-assembly, and membrane constriction.

Main Methods:

  • X-ray crystallography and cryo-electron microscopy were used to determine DSP structures.
  • Analysis of dimeric, tetrameric, and lipid-bound assemblies provided mechanistic insights.

Main Results:

  • Structural studies reveal how domain interactions and disordered regions regulate DSP self-assembly and GTPase activity.
  • Understanding transitions from cytosolic to membrane-bound states is crucial for helical constriction.

Conclusions:

  • DSP structure and regulation are critical for membrane remodeling and organelle dynamics.
  • Insights into DSP mechanisms offer potential for therapeutic strategies targeting DSP-related diseases.