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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 networks...

Actin Polymerization

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Protein Organization

Protein Organization

Protein Organization

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Generation of Straight or Branched Actin Filaments

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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
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Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been reported.

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Related Experiment Video

Updated: Jun 3, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Formation of framework nacre polypeptide supramolecular assemblies that nucleate polymorphs.

Fairland F Amos¹, Christopher B Ponce, John Spencer Evans

¹Laboratory for Chemical Physics, New York University, York, New York 10010, United States.

Biomacromolecules

|April 9, 2011

Summary

A specific nacre protein sequence (n16N) self-assembles into complexes that nucleate calcium carbonate crystals. These protein assemblies act as surfaces for crystal growth, potentially revealing a general biomineralization mechanism.

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Published on: November 2, 2011

Area of Science:

Biomineralization
Materials Science
Protein Self-Assembly

Background:

Mollusk shell nacre formation involves framework proteins interacting with β-chitin.
The precise control of crystal growth by nacre proteins remains poorly understood.
A short nacre protein sequence (n16N) previously showed varied calcium carbonate polymorph formation.

Purpose of the Study:

To investigate the self-assembly of the n16N sequence.
To determine how n16N influences calcium carbonate nucleation and polymorph formation.
To elucidate the role of n16N in biomineralization processes.

Main Methods:

Studied n16N self-assembly under varying pH conditions.
Investigated the effect of Ca(II) ions on n16N assembly.
Utilized Si wafers and polystyrene supports to analyze crystal nucleation on preassembled n16N structures.

Main Results:

n16N self-assembles into amorphous, nonmineralized supramolecular complexes.
These complexes nucleate calcium carbonate polymorphs (aragonite, vaterite, ACC) in vitro.
Preassembled n16N structures preferentially nucleated vaterite, indicating direct interaction with crystals.

Conclusions:

The n16N sequence forms supramolecular complexes that serve as nucleation sites for crystal growth.
This mechanism of protein-templated nucleation may be common among framework nacre proteins.
Understanding n16N assembly provides insights into controlling biomineral formation.