December 10, 2025

[Press Release] Simulations Reveal Protein "Dynamin" Constricts Cell Membranes by Loosening Its Grip

fig

Dynamin ring constricts the membrane by "loosening."
Dynamin assembles into a ring around the neck of a forming vesicle and utilizes GTP hydrolysis energy to constrict and sever the membrane. The simulation reveals that the dynamin ring expands (loosens) upon GTP hydrolysis, which indirectly forces the adjacent membrane tube to narrow.
Credit: Kei-ichi Okazaki
Restriction: CC BY

Release Summary

Computer simulations revealed the detailed mechanism of how the protein "dynamin" works to form small vesicles within cells.
While dynamin uses GTP hydrolysis energy to change shape, it was unclear how this leads to membrane constriction. Simulations showed that instead of simply tightening, dynamin "loosens" (expands) at a certain stage to generate the force needed to narrow the surrounding membrane tube.
This study provides a clearer explanation for membrane deformation and vesicle formation processes in cells, offering insights for artificial nano-device design.

For Details (Eurekalert!)

Information of the paper

  • Title: Membrane Constriction by Dynamin through GTP-Driven Conformational Changes from Coarse-Grained Molecular Dynamics Simulations
  • Authors: Md. Iqbal Mahmood, Shintaroh Kubo, Hiroshi Noguchi, and Kei-ichi Okazaki
  • Journal: The Journal of Physical Chemistry Letters
  • DOI: 10.1021/acs.jpclett.5c02867

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