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Microfilaments are usually about 7 nm in diameter and made up of two strands of actin. Microfilament functions include cytokinesis, amoeboid movement, cell motility, changes in cell shape, endocytosis and exocytosis, cell contractility, and mechanical stability. Microfilaments are flexible and relatively strong, resisting buckling by multi ...
Microfilament Polymerization. Microfilament polymerization is divided into three steps. The nucleation step is the first step, and it is the rate limiting and slowest step of the process. Elongation is the next step in this process, and it is the rapid addition of actin monomers at both the plus and minus end of the microfilament.
This is carried out by groups of highly specialized cells working together. A main component in the cytoskeleton that helps show the true function of this muscle contraction is the microfilament. Microfilaments are composed of the most abundant cellular protein known as actin. [10]
Together with an alpha-beta catenin complex, the cadherin can bind to the microfilaments of the cytoskeleton of the cell. This allows for homophilic cell–cell adhesion. [ 18 ] The β-catenin – α-catenin linked complex at the adherens junctions allows for the formation of a dynamic link to the actin cytoskeleton.
The functions of pseudopodia include locomotion and ingestion: Pseudopodia are critical in sensing targets which can then be engulfed; the engulfing pseudopodia are called phagocytosis pseudopodia. A common example of this type of amoeboid cell is the macrophage. They are also essential to amoeboid-like locomotion.
The cortex mainly functions to produce tension under the cell membrane, allowing the cell to change shape. [12] This is primarily accomplished through myosin II motors, which pull on the filaments to generate stress. [12] These changes in tension are required for the cell to change its shape as it undergoes cell migration and cell division. [12]
Rho Cascade - stress fiber formation. The Rho family of GTPases regulate many aspects of actin cytoskeletal dynamics, including stress fiber formation. RhoA (sometimes referred to as just 'Rho') is responsible for the formation of stress fibers, and its activity in stress fiber formation was first discovered by Ridley and Hall in 1992. [4]
ADF/cofilin is a family of actin-binding proteins associated with the rapid depolymerization of actin microfilaments that give actin its characteristic dynamic instability. [1] This dynamic instability is central to actin's role in muscle contraction, cell motility and transcription regulation.