Search results
Results From The WOW.Com Content Network
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.
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.
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.
Inside a cilium and a flagellum is a microtubule-based cytoskeleton called the axoneme. The axoneme of a primary cilium typically has a ring of nine outer microtubule doublets (called a 9+0 axoneme), and the axoneme of a motile cilium has two central microtubules in addition to the nine outer doublets (called a 9+2 axoneme).
Motor proteins utilizing the cytoskeleton for movement fall into two categories based on their substrate: microfilaments or microtubules. Actin motors such as myosin move along microfilaments through interaction with actin, and microtubule motors such as dynein and kinesin move along microtubules through interaction with tubulin.
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.
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 ]