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Actin Polymerization and Cell Motility

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Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
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Mechanism of Lamellipodia Formation

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Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...

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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Mechanism of Filopodia Formation

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Actin Polymerization

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Reconstitution of Actin-Based Motility with Commercially Available Proteins

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Directed actin polymerization is the driving force for epithelial cell-cell adhesion.

V Vasioukhin¹, C Bauer, M Yin

¹Department of Molecular Genetics and Cell Biology, Howard Hughes Medical Institute, The University of Chicago, Illinois 60637, USA.

|February 5, 2000

Summary

Epithelial cells use calcium-activated filopodia to embed into neighbors, forming adhesion zippers. This process requires alpha-catenin and VASP/Mena for actin reorganization to seal cell borders.

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Area of Science:

Cell biology
Molecular biology
Biophysics

Background:

Epithelial cells form tissues through intercellular adhesion.
Cadherin-mediated adhesion is crucial for tissue integrity.
The precise mechanisms of cell-cell adhesion dynamics are still being elucidated.

Purpose of the Study:

To investigate the novel roles of calcium and actin polymerization in cadherin-mediated intercellular adhesion.
To elucidate the molecular players and mechanisms involved in sealing epithelial cell borders.

Main Methods:

Live-cell imaging to observe filopodia dynamics and cell border sealing.
Genetic manipulation of alpha-catenin and VASP/Mena function in keratinocytes.
Immunofluorescence microscopy to visualize protein localization and actin organization.

Main Results:

Calcium stimulates filopodia that penetrate neighboring cells, clustering E-cadherin at tips.
A two-rowed zipper of puncta is formed, clamped by desmosomes.
Alpha-catenin, vinculin, zyxin, VASP, and Mena are recruited to adhesion zippers.
Actin reorganization and polymerization are essential for merging puncta and sealing cell borders.
Disruption of alpha-catenin or VASP/Mena function prevents membrane sealing.

Conclusions:

A dynamic mechanism of intercellular adhesion involving calcium-activated filopodia penetration and VASP/Mena-dependent actin reorganization is revealed.
Alpha-catenin and VASP/Mena are critical for the actin-based sealing of epithelial cell borders.
This study uncovers a novel pathway for establishing and maintaining epithelial tissue integrity.