cytoskeleton

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cytoskeleton

 [si″to-skel´ĕ-ton]
a conspicuous internal reinforcement in the cytoplasm of a cell, consisting of tonofibrils, filaments of the terminal web, and other microfilaments. adj., adj cytoskel´etal.

cy·to·skel·e·ton

(sī'tō-skel'ĕ-ton),
In cells, the microtubules and the filaments (thin, intermediate, and thick) that serve as supportive cytoplasmic elements to stiffen cells or to organize the location and movement of intracellular organelles.

cytoskeleton

(sī′tə-skĕl′ĭ-tn)
n.
The internal framework of a eukaryotic cell, composed of protein filaments that provide structural support and drive the movement of the cell and its internal components, typically divided into three categories (microfilaments, intermediate filaments, and microtubules) based on the diameter and composition of the filaments.

cy′to·skel′e·tal (-ĭ-tl) adj.

cy·to·skel·e·ton

(sī'tō-skel'ĕ-tŏn)
The tonofilaments, keratin, desmin, neurofilaments, or other intermediate filaments serving as supportive cytoplasmic elements to stiffen cells or to organize intracellular organelles.

cytoskeleton

A complex network of ACTIN filaments within the nucleated cell. Unlike the bony skeleton in vertebrates, this skeleton has contractile properties and can alter the shape, size and even movement, of the cell. The cytoskeleton is also concerned with the adhesion of adjacent cells.

cytoskeleton

a network of MICROTUBULES and MICROFILAMENTS in the cytoplasm of cells which is thought to give the cell its characteristic shape. The network enables the movement of specific organelles within the cytoplasm (as in vesicles produced by the GOLGI APPARATUS), and the production of general CYTOPLASMIC STREAMING.

cy·to·skel·e·ton

(sī'tō-skel'ĕ-tŏn)
The tonofilaments, keratin, desmin, neurofilaments, or other intermediate filaments serving as supportive cytoplasmic elements to stiffen cells or to organize intracellular organelles.
References in periodicals archive ?
All cytoskeletal proteins displayed strong immunoreactivity (Table).
The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. Cell 1988; 53(2):219-226.
Western blot analysis of GFL and axoplasm lysates indicate that, except for NF-220, cytoskeletal protein substrates are indeed present in both compartments (Fig.
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.[44] Although casein kinase I phosphorylates the cytoplasmic domain of band 3,[45] such phosphorylation would not be expected to lead to the kinetics seen in AD.[15,46] Furthermore, 2 groups have failed to detect AB in erythrocytes from patients with AD,[28,47] and phosphorylation of band 3 by this mechanism is not likely to contribute to abnormal anion exchange.
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).
Downregulated genes mainly revolved in protein binding (GO.0005515), binding (GO.0005488), cytoskeletal protein binding (GO.0008092), enzyme binding (GO.0019899), and nucleotide binding (GO.0000166) as shown in Table 2.
All identified proteins were clustered into the following seven categories (Figure 2A) based on information obtained from DAVID gene ontology (GO) database (http://david.abcc.ncifcrf.gov) and UniProt (http://www.uniprot.org): Catalytic activity (31%), ATPase activity (19%), oxidoreductase activity (13%), cytoskeletal protein binding (13%), actin binding (12%), calcium ion binding (6%) and structural constituent of muscle (6%) (Supplementary Table S1).
Furthermore, the brains of alcohol-fed animals had higher levels of the degradation products of a cytoskeletal protein called spectrin, which is degraded by calpains.
Alterations of cytoskeletal protein sulfhydryls and cellular glutathione in cultured cells exposed to cadmium and nickel ions.
Leroux, "Functional interaction between phosducin-like protein 2 and cytosolic chaperonin is essential for cytoskeletal protein function and cell cycle progression," Molecular Biology of the Cell, vol.
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.