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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.
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.
ADF/Cofilin family members bind G-actin monomers and depolymerize actin filaments through two mechanisms: severing [11] and increasing the off-rate for actin monomers from the pointed end. [12] "Older" ADP/ADP-Pi actin filaments free of tropomyosin and proper pH are required for cofilin to function effectively.
Cytochalasin is a toxin that will bind to the actin polymer, so it can no longer bind to the incoming actin monomers. Actin originally attached in the polymer is still leaving the microfilament causing depolymerization. Phalloidin is a toxin that will bind to actin locking the filament in place. Monomers are neither adding or leaving this ...
Alpha-actinin-2 is a 103.8 kDa protein composed of 894 amino acids. [6] [7] Each molecule is rod-shaped (35 nm in length) and it homodimerizes in an anti-parallel fashion.. Each monomer has an N-terminal actin-binding region composed of two calponin homology domains, two C-terminal EF hand domains, and four tandem spectrin-like repeats form the rod domain in the central region of the molecule.
The thick filament, myosin, has a double-headed structure, with the heads positioned at opposite ends of the molecule. During muscle contraction, the heads of the myosin filaments attach to oppositely oriented thin filaments, actin, and pull them past one another. The action of myosin attachment and actin movement results in sarcomere shortening.
These filaments are made of two strands of actin monomers (or protofilaments) wrapping around each other, to create a single actin filament. Because actin monomers are not symmetrical molecules, their filaments have polarity based upon the structure of the actin monomer, which will allow one end of the actin filament to polymerize faster than ...
It functions as a modulator of membrane behavior and cell surface properties. [1] [2] [3] In most eukaryotic cells lacking a cell wall, the cortex is an actin-rich network consisting of F-actin filaments, myosin motors, and actin-binding proteins.