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stress fiber
Stress fibers are contractile actin bundles found in non-muscle cells. They are composed of actin (microfilaments) and non-muscle myosin II (NMMII), and also contain various crosslinking proteins, such as α-actinin, to form a highly regulated actomyosin structure within non-muscle cells. Stress fibers have been shown to play an important role in cellular contractility, providing force for a number of functions such as cell adhesion, migration and morphogenesis.
==Structure==
Stress fibers are primarily composed of actin and myosin. Actin is a ~43kDa globular protein, and can polymerize to form long filamentous structures.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 the other. The end that can polymerize faster is known as the plus-end, whereas the end that polymerizes slower is known as the minus-end. Stress fibers are usually composed of 10-30 actin filaments. Stress fibers are composed of antiparallel microfilaments: actin filaments are bundled along their length, and plus-ends and minus-ends co-mingle at each end of the bundle. The antiparallel arrangement of actin filaments within stress fibers is reinforced by α-actinin, an actin filament crosslinking protein which contains antiparallel actin-binding domains. These bundles are then cross-linked by NMMII to form stress fibers.
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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