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ACTA2 (actin alpha 2) is an actin protein with several aliases including alpha-actin, alpha-actin-2, aortic smooth muscle or alpha smooth muscle actin (α-SMA, SMactin, alpha-SM-actin, ASMA). Actins are a family of globular multi-functional proteins that form microfilaments .
Actin, alpha skeletal muscle is a protein that in humans is encoded by the ACTA1 gene. [5] [6] Actin alpha 1 which is expressed in skeletal muscle is one of six different actin isoforms which have been identified. Actins are highly conserved proteins that are involved in cell motility, structure and integrity.
A gene duplication resulted in the emergence of a stable lineage that led to modern alpha-actinin genes. Simultaneously, the other duplicated gene acquired extra repeats through a series of unequal crossing-over events. This made the spectrin subunit ancestor which is an antiparallel homodimer that can crosslink actin filaments. [3]
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.
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.
Actin, cytoplasmic 2, or gamma-actin is a protein that in humans is encoded by the ACTG1 gene. [5] Gamma-actin is widely expressed in cellular cytoskeletons of many tissues; in adult striated muscle cells, gamma-actin is localized to Z-discs and costamere structures, which are responsible for force transduction and transmission in muscle cells.
Profilin is an actin-binding protein involved in the dynamic turnover and reconstruction of the actin cytoskeleton. [1] It is found in most eukaryotic organisms. Profilin is important for spatially and temporally controlled growth of actin microfilaments, which is an essential process in cellular locomotion and cell shape changes.
When calcium binds to the troponin C, it causes conformational changes which lead to dislocation of troponin I. Afterwards, tropomyosin leaves the binding site for myosin on actin leading to contraction of muscle. The letter I is given due to its inhibitory character. It is a useful marker in the laboratory diagnosis of heart attack. [2]