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A merged stack of confocal images showing actin filaments within a cell. The image has been colour coded in the z axis to show in a 2D image which heights filaments can be found at within cells. Periodic actin rings - A periodic structure constructed of evenly spaced actin rings is found in axons. [12]
Filament cross-linkers (e.g., α-actinin, fascin, and fimbrin) Actin monomer-binding proteins profilin and thymosin β4; Filament barbed-end cappers such as Capping Protein and CapG, etc. Filament-severing proteins like gelsolin. Actin depolymerizing proteins such as ADF/cofilin. The actin filament network in non-muscle cells is highly dynamic.
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These filament forming proteins have been classified into 4 classes. Tubulin-like, actin-like, Walker A cytoskeletal ATPases (WACA-proteins), and intermediate filaments. [8] [28] Tubulin-like proteins are tubulin in eukaryotes and FtsZ, TubZ, RepX in prokaryotes. Actin-like proteins are actin in eukaryotes and MreB, FtsA in prokaryotes.
The actin filaments depolymerize and disassemble on the proximal end to allow free monomers to migrate to the leading edge (distal end) of the actin filament where it can polymerize and thus reattach. Actin filaments are also constantly being transported away from the leading edge by a myosin-motor driven process known as retrograde F-actin flow.
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 ...
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Thick filaments consist primarily of the protein myosin, that is responsible for force generation. It is composed of a globular head with both ATP and actin binding sites, and a long tail involved in its polymerization into myosin filaments. Elastic filaments are made up of a giant protein called titin and hold the thick filaments in place.
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