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Related Experiment Video

Updated: May 29, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

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Published on: January 11, 2017

The crystal structure of dynamin.

Marijn G J Ford¹, Simon Jenni, Jodi Nunnari

¹Department of Molecular and Cellular Biology, University of California, Davis, Davis, California 95616, USA.

|September 20, 2011

Summary

Dynamin-related proteins (DRPs) are crucial for membrane remodeling. This study reveals the structure of dynamin 1, offering insights into how DRPs self-assemble and drive membrane scission events.

Area of Science:

Biochemistry
Cell Biology
Structural Biology

Background:

Dynamin-related proteins (DRPs) are essential GTPases involved in membrane dynamics.
The mechanisms by which DRPs self-assemble and alter membrane structure remain unclear.

Purpose of the Study:

To elucidate the structural basis of dynamin 1 assembly and its role in membrane remodeling.
To understand the molecular mechanisms underlying DRP-mediated membrane scission.

Main Methods:

X-ray crystallography was used to determine the structure of nucleotide-free mammalian dynamin 1 (lacking the proline-rich domain).
Structural analysis focused on monomeric and oligomeric states, particularly interfaces involved in dimerization and multimerization.

Main Results:

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Published on: November 30, 2018

The crystal structure of assembly-deficient dynamin 1 in its nucleotide-free state was determined.
The monomer exhibits an extended conformation with distinct domains (GTPase, bundle signaling element, helical stalk, pleckstrin homology domain).
Dimerization and higher-order multimer formation occur through interfaces within the helical stalk, providing insights into DRP specificity and regulation.

Conclusions:

The determined structure provides a framework for understanding DRP self-assembly and higher-order structure biogenesis.
These findings offer insights into the mechanism of DRP-mediated membrane scission events.
The study highlights the importance of stalk interfaces in DRP function and regulation.