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Related Concept Videos

Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.5K
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...
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Generation of Straight or Branched Actin Filaments01:14

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
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
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Actin Polymerization and Cell Motility01:13

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.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
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Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Introduction to Actin01:26

Introduction to Actin

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Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across...
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Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
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Updated: Dec 28, 2025

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
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Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops

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Dimensionality changes actin network through lamin A/C and zyxin.

Jip Zonderland1, Ivan Lorenzo Moldero1, Shivesh Anand1

  • 1Complex Tissue Regeneration Department, MERLN Institute for Technology-Inspired Regenerative Medicine, Maastricht University, Universiteitssingel 40, 6229 ET, Maastricht, the Netherlands.

Biomaterials
|February 23, 2020
PubMed
Summary
This summary is machine-generated.

Three-dimensional (3D) environments, unlike 2D cultures, prevent human mesenchymal stromal cells (hMSCs) from building cellular tension, impacting mechanosensing proteins and actin cytoskeleton regulation in tissue engineering scaffolds.

Keywords:
ActinDimensionalityLaminMesenchymal stromal cellsZyxin

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Area of Science:

  • Biomaterials Science
  • Cell Biology
  • Tissue Engineering

Background:

  • Mechanosensing protein regulation is crucial for tissue engineering but poorly understood in 3D environments.
  • The actin cytoskeleton's role in human mesenchymal stromal cells (hMSCs) is vital but understudied in 3D scaffolds.
  • Existing research primarily focuses on 2D culture platforms, limiting insights into 3D cellular behavior.

Purpose of the Study:

  • To investigate the regulation of mechanosensing proteins and the actin cytoskeleton in hMSCs within 3D tissue-engineered scaffolds.
  • To compare hMSC behavior on 3D scaffolds versus 2D films of the same material.
  • To elucidate the role of lamin A/C and zyxin in 3D cellular tension and lineage commitment.

Main Methods:

  • Culturing hMSCs on 3D electrospun and additive manufactured scaffolds and 2D films.
  • Assessing actin stress fiber formation, focal adhesions, and YAP1 nuclear localization.
  • Measuring lamin A/C expression, myosin light chain phosphorylation, and zyxin knockdown effects.
  • Evaluating osteogenic lineage commitment in 3D constructs.

Main Results:

  • hMSCs on 3D scaffolds showed reduced actin stress fibers, focal adhesions, lamin A/C expression, YAP1 nuclear localization, and myosin light chain phosphorylation compared to 2D cultures.
  • Dimensionality, not material stiffness, was identified as the primary factor preventing cellular tension buildup in 3D.
  • Knockdown of lamin A/C or zyxin reduced stress fibers, with zyxin influencing lamin A/C expression, indicating an external signaling pathway.
  • Osteogenic lineage commitment was unaffected by the altered mechanosensing protein expression in 3D.

Conclusions:

  • 3D environments significantly alter hMSC mechanosensing and actin cytoskeleton organization compared to 2D cultures, primarily by inhibiting cellular tension.
  • Lamin A/C and zyxin play key roles in mediating the effects of dimensionality on the actin cytoskeleton in hMSCs.
  • These findings have critical implications for designing effective tissue engineering scaffolds for both stiff and soft tissues.
  • Cellular response to dimensionality differs from material properties, impacting future scaffold design strategies.