actin

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actin,

a protein abundantly present in many cells, especially muscle cells, that significantly contributes to the cell's structure and motility. Actin can very quickly assemble into long polymer rods called microfilaments. These microfilaments have a variety of roles—they form part of the cell's cytoskeleton, they interact with myosinmyosin
, one of the two major protein constituents responsible for contraction of muscle. In muscle cells myosin is arranged in long filaments called thick filaments that lie parallel to the microfilaments of actin.
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 to permit movement of the cell, and they pinch the cell into two during cell division. In muscle contraction, filaments of actin and myosin alternately unlink and chemically link in a sliding action. The energy for this reaction is supplied by adenosine triphosphateadenosine triphosphate
(ATP) , organic compound composed of adenine, the sugar ribose, and three phosphate groups. ATP serves as the major energy source within the cell to drive a number of biological processes such as photosynthesis, muscle contraction, and the synthesis of
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.

actin

[′ak·tən]
(biochemistry)
A muscle protein that is the chief constituent of the Z-band myofilaments of each sarcomere.
References in periodicals archive ?
Actin participates in many protein-protein interactions, including self-association of actin to form F-actin.
2+], gelsolin severs and caps polymeric actin filaments (F-actin) (21): after binding of domain G1 and partly domain G2 to the actin filament (F-actin), gelsolin rapidly severs F-actin and then remains bound to the barbed end of one of the newly formed filaments, forming a stable cap, thus inhibiting addition of further monomers.
The concentration of gelsolin seems to be rate limiting in the actin removal system and depends on the rates of formation, dissociation, and clearance of the actin-gelsolin complex.
In addition to scavenging of actin, Gc-globulin also plays additional roles in some non-actin-scavenging functions (Fig.