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Assembly of Cytoskeletal Filaments

Assembly of Cytoskeletal Filaments

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...

Actin Polymerization

Actin Polymerization

Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶ nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight actin...

The Role of Actin and Myosin in Non-muscle Cells

The Role of Actin and Myosin in Non-muscle Cells

Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They are held...

Introduction to Actin

Introduction to Actin

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 different species.

Actin Polymerization and Cell Motility

Actin Polymerization and Cell Motility

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.

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...

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Biomimetic F-actin cortex models.

Tamás Haraszti¹, Anabel E-M Clemen, Joachim P Spatz

¹Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, Im Neuenhelmer Feld 253, 69120 Heidelberg, Germany. tamas.haraszti@uni-heidelberg.de

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|October 13, 2009

Summary

Actin, initially a muscle protein, is now key to cytoskeleton functions like cell motility. In vitro models simplify actin networks, aiding the construction of complex biological systems.

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Area of Science:

Biochemistry
Cell Biology
Biophysics

Background:

Actin's role has evolved from muscle protein to essential cytoskeleton component.
It is crucial for cell motility, adhesion, morphology, and intracellular transport.
In vitro models have been developed for two decades to study actin networks' properties.

Purpose of the Study:

To review the development of in vitro actin network models.
To highlight their application in constructing complex biological systems.

Main Methods:

Review of existing literature on actin network models.
Analysis of model complexity, from single filaments to microfluidic networks.

Main Results:

Actin's known functions have expanded significantly beyond muscle tissue.
In vitro models range from simple F-actin filaments to complex suspended networks.
These models allow for controlled investigation of actin network chemophysical and biomechanical properties.

Conclusions:

In vitro actin models have advanced our understanding of cytoskeleton dynamics.
These models are instrumental in building systems that mimic cellular cortex structures.