16 Facts About Actin


Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils.

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Actin participates in many important cellular processes, including muscle contraction, cell motility, cell division and cytokinesis, vesicle and organelle movement, cell signaling, and the establishment and maintenance of cell junctions and cell shape.

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Actin therefore contributes to processes such as the intracellular transport of vesicles and organelles as well as muscular contraction and cellular migration.

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Actin protein is found in both the cytoplasm and the cell nucleus.

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Actin's cytoskeleton is key to the processes of endocytosis, cytokinesis, determination of cell polarity and morphogenesis in yeasts.

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Actin networks are distributed throughout the cytoplasm of cells that have been cultivated in vitro.

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Actin is involved in the movement of organelles and in cellular morphogenesis, which involve cell division as well as the elongation and differentiation of the cell.

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Actin is exported at least in two ways, through exportin 1 and exportin 6.

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Actin plays a particularly prominent role in muscle cells, which consist largely of repeated bundles of actin and myosin II.

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Actin has specific binding sequences, which interact with the d and ß-CCT subunits or with d-CCT and e-CCT.

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Actin is an ATPase, which means that it is an enzyme that hydrolyzes ATP.

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Actin filaments are often rapidly assembled and disassembled, allowing them to generate force and support cell movement.

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Actin branching at the cell membrane is important for cell movement, and so the plasma membrane lipid PIP2 activates the nucleation promoting factor WASp and inhibits CapZ.

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Actin is one of the most conserved proteins throughout the evolution of eukaryotes.

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Actin is used in scientific and technological laboratories as a track for molecular motors such as myosin and as a necessary component for cellular functioning.

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Actin was first observed experimentally in 1887 by W D Halliburton, who extracted a protein from muscle that 'coagulated' preparations of myosin that he called "myosin-ferment".

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