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Related Experiment Videos

Structural conversion between open and closed forms of radixin: low-angle shadowing electron microscopy.

H Ishikawa1, A Tamura, T Matsui

  • 1Department of Cell Biology, Faculty of Medicine, Kyoto University, Japan.

Journal of Molecular Biology
|August 15, 2001
PubMed
Summary

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Ezrin/radixin/moesin (ERM) proteins switch between inactive, closed forms and active, open forms. This conformational change, visualized by electron microscopy, is crucial for their function as cross-linkers in cells.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Structural Biology

Background:

  • Ezrin/radixin/moesin (ERM) proteins link actin filaments to the plasma membrane.
  • Their function is regulated by conformational changes between active and inactive states, influenced by Rho signaling and C-terminal phosphorylation.

Purpose of the Study:

  • To directly visualize the conformational changes between active and inactive ERM proteins.
  • To investigate the structural differences between wild-type, non-phosphorylated (T564A), and phosphorylated (T564E) radixin.

Main Methods:

  • Low-angle rotary-shadowing electron microscopy was used to examine radixin molecules.
  • Analysis of wild-type, T564A, and T564E radixin conformations.

Main Results:

Related Experiment Videos

  • T564A and wild-type radixin exhibited globular, closed forms (8-14 nm).
  • T564E radixin displayed elongated, open forms with distinct globular structures (approx. 8 nm and 5 nm) linked by filamentous structures (20-25 nm).

Conclusions:

  • The closed and open forms correspond to the inactive and active states of radixin, respectively.
  • Phosphorylation at T564 is critical for stabilizing the active, open conformation of radixin, enabling its function as a cross-linker.