Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Formation of Higher-order Actin Filaments

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Author Correction: Progerinin, an optimized progerin-lamin A binding inhibitor, ameliorates premature senescence phenotypes of Hutchinson-Gilford progeria syndrome.

Communications biology·2026

Same author

Obesity history exacerbates liver macrophage-mediated fibrosis via IGFBP7.

Biochimica et biophysica acta. Molecular basis of disease·2026

Same author

Family-Specialized Transformer for L-cystathionine gamma-lyase Engineering and Its Structural Interpretation.

Computational and structural biotechnology journal·2026

Same author

Diol-enhanced natural deep eutectic solvents for efficient poplar pretreatment.

Frontiers in chemistry·2026

Same author

Mechanism by which a linoleic acid metabolite suppresses cancer cell growth by inhibiting mTOR.

Cell chemical biology·2026

Same author

Application of adipose-derived mesenchymal stem cell 3D structure, Microblock, as a skin regeneration therapy.

European journal of pharmacology·2026

Search research articles

Related Experiment Video

Updated: Jan 5, 2026

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

Published on: May 16, 2017

High-resolution structures of annexin A5 in a two-dimensional array.

Seokho Hong¹, Soohui Na¹, Ok-Hee Kim²

¹Department of Agricultural Biotechnology, Research Institute of Agriculture and Life Sciences, Center for Food and Bioconvergence, Center for Food Safety and Toxicology, Seoul National University, Seoul 08826, Republic of Korea.

Journal of Structural Biology

|October 13, 2019

Summary

Annexin A5 proteins form 2D arrays on cell membranes, preventing rupture. This study reveals the molecular basis of calcium-dependent assembly and membrane interaction for annexins.

Keywords:

Annexin Crystal structure Membrane rupture Two-dimensional array

More Related Videos

Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies

Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies

Published on: November 20, 2021

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Related Experiment Videos

Last Updated: Jan 5, 2026

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

Published on: May 16, 2017

Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies

Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies

Published on: November 20, 2021

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Area of Science:

Biochemistry
Structural Biology
Cell Biology

Background:

Annexins are cytosolic proteins that bind to cell membranes.
Annexin A5 self-assembles into a 2D array, attaching to damaged membranes to prevent cell rupture.
The molecular mechanisms underlying annexin A5's membrane interaction and assembly are not fully understood.

Purpose of the Study:

To elucidate the molecular mechanisms of annexin A5 self-assembly and membrane binding.
To determine the high-resolution crystal structures of annexin A5 with and without calcium (Ca2+).
To provide molecular insights into how annexins modulate cell membrane properties.

Main Methods:

X-ray crystallography was used to determine the crystal structures of annexin A5 in the presence and absence of Ca2+.
Structural analysis focused on the Ca2+-dependent motion of a tryptophan residue and protein-protein interactions.
Comparison of high-resolution structures with low-resolution imaging data and existing knowledge.

Main Results:

The crystal structures revealed a conserved crystal packing and a 2D arrangement into a p3 lattice for annexin A5, consistent with low-resolution data.
Calcium binding induces an outward motion of a tryptophan residue, crucial for the p3 lattice formation.
A three-fold interaction near the tryptophan residue was identified as key for mediating p3 lattice formation.
A hypothesis suggests phosphatidyl serine (PS) promotes p3 lattice formation.

Conclusions:

This study provides high-resolution structural data clarifying the Ca2+-dependent assembly of annexin A5 into a 2D p3 lattice.
The findings offer molecular insights into how annexin A5 modulates cell membrane physical properties based on Ca2+ concentration and phospholipid composition.
The research enhances understanding of annexin function in membrane stabilization and repair.