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A system of filaments found in the cytoplasm of cells and responsible for the maintenance of and changes in cell shape, cell locomotion, movement of various elements in the cytoplasm, integration of the major cytoplasmic organelles, cell division, chromosome organization and movement, and the adhesion of a cell to a surface or to other cells.

Three major classes of filaments have been resolved on the basis of their diameter and cytoplasmic distribution: actin filaments (or microfilaments) each with an average diameter of 6 nanometers, microtubules with an average diameter of 25 nm, and intermediate filaments whose diameter of 10 nm is intermediate to that of the other two classes. The presence of this system of filaments in all cells, as well as their diversity in structure and cytoplasmic distribution, has been recognized only in the modern period of biology.

A technique that has greatly facilitated the visualization of these filaments, as well as the analysis of their chemical composition, is immunofluorescence applied to cells grown in tissue culture. See Immunofluorescence

Actin is the main structural component of actin filaments in all cell types, both muscle and nonmuscle. Actin filaments assume a variety of configurations depending on the type of cell and the state it is in. They extend a considerable distance through the cytoplasm in the form of bundles, also known as stress fibers since they are important in determining the elongated shape of the cell and in enabling the cell to adhere to the substrate and spread out on it. Actin filaments can exist in forms other than straight bundles. In rounded cells that do not adhere strongly to the substrate (such as dividing cells and cancer cells), the filaments form an amorphous meshwork that is quite distinct from the highly organized bundles. The two filamentous states, actin filament bundles and actin filament meshworks, are interconvertible polymeric states of the same molecule. Bundles give the cell its tensile strength, adhesive capability, and structural support, while meshworks provide elastic support and force for cell locomotion.

Microtubules are slender cylindrical structures that exhibit a cytoplasmic distribution distinct from actin filaments. Microtubules originate in structures that are closely associated with the outside surface of the nucleus known as centrioles. The major structural protein of these filaments is known as tubulin. Unlike the other two classes of filaments, microtubules are highly unstable structures and appear to be in a constant state of polymerization-depolymerization. See Centriole

Intermediate filaments function as the true cytoskeleton. Unlike microtubules and actin filaments, intermediate filaments are very stable structures. They have a cytoplasmic distribution independent of actin filaments and microtubules. In the intact cell, they anchor the nucleus, positioning it within the cytoplasmic space. During mitosis, they form a filamentous cage around the mitotic spindle which holds the spindle in a fixed place during chromosome movement.


(cell and molecular biology)
Protein fibers composing the structural framework of a cell.
References in periodicals archive ?
The effect of ageing on the water-holding capacity of pork: Role of cytoskeletal proteins.
8-11) Dystrophin is a subsarcolemmal protein of the caveolar domain with a double adhesion property, one between the membrane elements and the contractile filaments and the other between the cytoskeletal proteins and the extracellular matrix via the laminin-binding system.
The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein.
Western blot analysis of GFL and axoplasm lysates indicate that, except for NF-220, cytoskeletal protein substrates are indeed present in both compartments (Fig.
Because calpains are responsible for the proteolysis of cytoskeletal proteins, investigators have suggested that calpain activity is involved in modulating cell structure in both normal and pathological states.
Phosphorylation of membrane-associated cytoskeletal proteins affects red blood cell shape, and a disruption of the normal pattern of phosphorylation may contribute to the formation of acanthocytes.
Several host cytoskeletal proteins are involved in tail formation, including [Alpha]-actinin (48), filamin (59), fimbrin (59), vasodilator-stimulated phosphoprotein (VASP) (60), vinculin (49,61), and neural-Wiskott-Aldrich syndrome protein (N-WASP) (63).
Because PC12 cells are particularly rich in cytoskeletal proteins (16) and because SLE patients may present serum antibodies against these proteins (17), it is likely that the positivity of the two SLE serum samples was caused by the recognition by antibodies of non-AChR proteins, probably cytoskeletal proteins.
A ATPase activity 19% oxidoreductase activity 13% cytoskeletal protein binding 13% actin binding 12% Structural consttuent of muscle 6% calcium ion binding 6% catalytic activity 31% B Actin binding 40% Structurral consituent of muscle 20% Cytoskeletal protein binding 40% C Cellublar metabolic process 26% Primary metabolic process 26% Catabolic process 18% Nitrogen compound metabolic process 19% Oxidation reduction 11% Note: Table made from pie chart.
As a component of focal adhesions, Testin interacts with the cytoskeletal protein such as zyxin, talin, vasodilator-stimulated phosphoprotein, Mena, extractable nucler antigen (EVL), alphall-spectrin, actin and actin-related proteins 7A.
Alterations of cytoskeletal protein sulfhydryls and cellular glutathione in cultured cells exposed to cadmium and nickel ions.
Further, they proposed that TCP 1 protein has a role in the remodeling of cytoskeletal protein like actin and tubulin (Kim et al.