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microfilament
Microfilaments or actin filaments are the thinnest filaments of the cytoskeleton, a structure found in the cytoplasm of eukaryotic cells. These linear polymers of actin subunits are flexible and relatively strong, resisting buckling by multi-piconewton compressive forces and filament fracture by nanonewton tensile forces. Microfilaments are highly versatile, functioning in cytokinesis, amoeboid movement, and changes in cell shape. In inducing this cell motility, one end of the actin filament elongates while the other end contracts, presumably by myosin II molecular motors.〔Keith Roberts, Martin Raff, Bruce Alberts, Peter Walter, Julian Lewis and Alexander Johnson, ''Molecular Biology of the Cell'', 4th Edition, Routledge, March 2002, hardcover, 1616 pages, 7.6 pounds, ISBN 0-8153-3218-1〕 Additionally, they function as part of actomyosin-driven contractile molecular motors, wherein the thin filaments serve as tensile platforms for myosin's ATP-dependent pulling action in muscle contraction and pseudopod advancement. Microfilaments have a tough, flexible framework which helps the cell in movement.
==Organization==
Actin filaments are assembled in two general types of structures: bundles and networks. Bundles can be composed of polar filament arrays, in which all barbed ends point to the same end of the bundle, or non-polar arrays, where the barbed ends point towards both ends. A class of actin-binding proteins, called cross-linking proteins, dictate the formation of these structures. Cross-linking proteins determine filament orientation and spacing in the bundles and networks. These structures are regulated by many other classes of actin-binding proteins, including motor proteins, branching proteins, severing proteins, polymerization promoters, and capping proteins.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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