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Typus
Verschleierung
Bearbeiter
Graf Isolan
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 32, Zeilen: 6-21
Quelle: Ziegler et al 2006
Seite(n): 453, 458, Zeilen: 453: li.Sp. 1-5; 458: re.Sp. 1-16.21-24
1.4.2. Vinculin and cytoskeleton protein Actin in cell migration

Vinculin is a ubiquitously expressed actin-binding protein. It [sic!] used as a marker for both cell–cell and cell–extracellular matrix (focal adhesion) adherens-type junctions, but its function has remained elusive. A variety of phenotypes of Vinculin-null cells have been shown that the role for vinculin include cell adhesion, cell spreading, focal adhesion stability and strengthening, cell migration and resistance to apoptosis. Vinculin regulate the focal adhesion dynamics, and that transient increases in local phosphoinositide levels. This effect inhibits the vinculin–F-actin interaction, promote focal adhesion turnover and cell motility. Interestingly, the muscle-specific splice variant of vinculin called metavinculin (which contains a 68 amino acid insert in the Vt domain), is localized in dense plaques and costameres, cell–extracellular matrix junctions that are much longer lived than focal adhesions. It could be significant that the Vt/D5 domain of metavinculin interacts less strongly with acidic phospholipids than does the Vt/D5 domain of vinculin [S. Witt et al., 2004]. The association of metavinculin–vinculin heterodimers with F-actin might therefore be relatively resistant to phospholipid competition.


Witt S, Zieseniss A, Fock U, Jockusch BM, Illenberger S. (2004). Comparative biochemical analysis suggests that vinculin and metavinculin cooperate in muscular adhesion sites, J. Biol. Chem. 279 pp. 31533–31543.

[Seite 453]

Vinculin is a ubiquitously expressed actin-binding protein frequently used as a marker for both cell–cell and cell–extracellular matrix (focal adhesion) adherens-type junctions, but its function has remained elusive. [...]


[Seite 458]

These results suggest a model in which focal adhesion dynamics is regulated by vinculin, and that transient increases in local phosphoinositide levels, which inhibit the vinculin–F-actin interaction, promote focal adhesion turnover and cell motility (Figure 2c). Interestingly, the muscle-specific splice variant of vinculin called metavinculin (which contains a 68 amino acid insert in the Vt domain), is localized in dense plaques and costameres, cell–extracellular matrix junctions that are much longer lived than focal adhesions. It could be significant that the Vt/D5 domain of metavinculin interacts less strongly with acidic phospholipids than does the Vt/D5 domain of vinculin [65]. The association of metavinculin–vinculin heterodimers with F-actin might therefore be relatively resistant to phospholipid competition, resulting in more persistent adhesions.

Conclusions

[...] Vinculin-null cells show a variety of phenotypes that clearly indicate a role for vinculin in cell adhesion, cell spreading, focal adhesion stability and strengthening, cell migration and resistance to apoptosis.


65 Witt, S. et al. (2004) Comparative biochemical analysis suggests that vinculin and metavinculin cooperate in muscular adhesion sites. J. Biol. Chem. 279, 31533–31543

Anmerkungen

Ohne Hinweis auf eine Übernahme. Beim leicht anpassenden Kopieren ist ein Fehler im Satzbau entstanden, als das eigentlich erforderliche is weggelassen wurde.

Sichter
(Graf Isolan), SleepyHollow02

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