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Microfilaments, also called actin filaments, are protein filaments in the cytoplasm of eukaryotic cells that form part of the cytoskeleton. They are primarily composed of polymers of actin , but are modified by and interact with numerous other proteins in the cell.
The cytoskeleton consists of (a) microtubules, (b) microfilaments, and (c) intermediate filaments. [1]The cytoskeleton is a complex, dynamic network of interlinking protein filaments present in the cytoplasm of all cells, including those of bacteria and archaea. [2]
Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils.It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm.
Compared to the other parts of the cytoskeletons, the microfilaments contain the thinnest filaments, with a diameter of approximately 7 nm. Microfilaments are part of the cytoskeleton that are composed of protein called actin. Two strands of actin intertwined together form a filamentous structure allowing for the movement of motor proteins.
Within the lamellipodia are ribs of actin called microspikes, which, when they spread beyond the lamellipodium frontier, are called filopodia. [2] The lamellipodium is born of actin nucleation in the plasma membrane of the cell [ 1 ] and is the primary area of actin incorporation or microfilament formation of the cell.
A myofibril (also known as a muscle fibril or sarcostyle) [1] is a basic rod-like organelle of a muscle cell. [2] Skeletal muscles are composed of long, tubular cells known as muscle fibers, and these cells contain many chains of myofibrils. [3] Each myofibril has a diameter of 1–2 micrometres. [3]
The second class is composed of MAPs with a molecular weight of 200-1000 kDa, of which there are four known types: MAP-1, MAP-2, MAP-3 and MAP-4. MAP-1 proteins consists of a set of three different proteins: A, B and C. The C protein plays an important role in the retrograde transport of vesicles and is also known as cytoplasmic dynein. MAP-2 ...
Furthermore, like tubulin, monomeric FtsZ is bound to GTP and polymerizes with other FtsZ monomers with the hydrolysis of GTP in a mechanism similar to tubulin dimerization. [10] Since FtsZ is essential for cell division in bacteria, this protein is a target for the design of new antibiotics . [ 11 ]