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Angaben zur Quelle [Bearbeiten]

Autor     Miguel Vicente-Manzanares, Colin Kiwon Choi und Alan Rick Horwitz
Titel    Integrins in cell migration – the actin connection
Zeitschrift    Journal of Cell Science
Herausgeber    The Company of Biologists
Ausgabe    122
Jahr    2009
Seiten    199-206
Anmerkung    PubMed ID: 19118212
DOI    10.1242/jcs.018564
URL    http://jcs.biologists.org/content/122/2/199.full

Literaturverz.   

nein
Fußnoten    nein
Fragmente    2


Fragmente der Quelle:
[1.] Shg/Fragment 033 23 - Diskussion
Zuletzt bearbeitet: 2014-11-01 15:26:28 Singulus
Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Shg, Vicente-Manzanares et al 2009

Typus
KomplettPlagiat
Bearbeiter
Graf Isolan
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 33, Zeilen: 23-32
Quelle: Vicente-Manzanares et al 2009
Seite(n): 201, 202, Zeilen: 201: re.Sp. 25-34; 202: li.Sp. 3-9
Actin polymerization and adhesion formation are linked. Actin polymerization determines the rate of adhesion assembly and potentially nucleates adhesions that contain activated integrins; conversely, adhesions provide nucleation points that may support actin polymerization. Adhesions and actin are also physically linked and this linkage coordinates adhesion assembly and disassembly and the processes they regulate. Adhesion assembly requires actin polymerization suggesting that the interaction of a subset of adhesion components with actin nucleates the nascent adhesion, which is then stabilized by its association with integrins. The direct interaction of focal adhesion kinase (FAK) and vinculin with the Arp2/3 complex [DeMali et al., 2002; Serrels et al., 2007], the main [nucleator of actin branching and polymerization in lamellipodia, constitutes a possible mechanism for targeting vinculin and FAK to future adhesion sites.]

DeMali, K. A., Barlow, C. A. and Burridge, K. (2002). Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J. Cell Biol. 159, 881-891.

Serrels, B., Serrels, A., Brunton, V. G., Holt, M., McLean, G. W., Gray, C. H., Jones, G. E. and Frame, M. C. (2007). Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex. Nat. Cell Biol. 9, 1046-1056.

[Seite 201]

However, the observation that adhesion assembly requires actin polymerization suggests that the interaction of a subset of adhesion components with actin nucleates the nascent adhesion, which is then stabilized by its association with integrins. In this context, the direct interaction of focal adhesion kinase (FAK) and vinculin with the Arp2/3 complex (DeMali et al., 2002; Serrels et al., 2007), the main nucleator of actin branching and polymerization in lamellipodia, constitutes a possible mechanism for targeting vinculin and FAK to future adhesion sites.

[Seite 202]

Thus, actin polymerization and adhesion formation are linked. Actin polymerization determines the rate of adhesion assembly and potentially nucleates adhesions that contain activated integrins; conversely, adhesions provide nucleation points that may support actin polymerization. Adhesions and actin are also physically linked and this linkage coordinates adhesion assembly and disassembly and the processes they regulate.


DeMali, K. A., Barlow, C. A. and Burridge, K. (2002). Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J. Cell Biol. 159, 881-891.

Serrels, B., Serrels, A., Brunton, V. G., Holt, M., McLean, G. W., Gray, C. H., Jones, G. E. and Frame, M. C. (2007). Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex. Nat. Cell Biol. 9, 1046-1056.

Anmerkungen

Ohne Hinweis auf eine Übernahme.

Sichter
(Graf Isolan), SleepyHollow02

[2.] Shg/Fragment 034 01 - Diskussion
Zuletzt bearbeitet: 2014-11-01 21:16:10 Singulus
Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Shg, Vicente-Manzanares et al 2009

Typus
KomplettPlagiat
Bearbeiter
Graf Isolan
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 34, Zeilen: 1-12
Quelle: Vicente-Manzanares et al 2009
Seite(n): 201-202, Zeilen: 201: re.Sp. 29-44 - 202: li.Sp. 1 ff.
[The direct interaction of focal adhesion kinase (FAK) and vinculin with the Arp2/3 complex [DeMali et al., 2002; Serrels et al., 2007], the main] nucleator of actin branching and polymerization in lamellipodia, constitutes a possible mechanism for targeting vinculin and FAK to future adhesion sites. The presence of activated integrins in regions of protrusion outside adhesions suggests that they enter the forming adhesion in an activated state [Galbraith et al., 2007; Kiosses et al., 2001]. The other implication is that adhesions might nucleate actin polymerization. This would provide a mechanism for the formation of actin filaments on which adhesions elongate; these appear to elongate from nascent adhesions at the lamellipodium-lamellum interface. This possibility is supported by the observation that purified integrin-adhesion complexes have actin-polymerization activity [Butler et al., 2006]. Although the neutralization of Arp2/3 in β3-integrin-containing adhesion complexes did not impair actin polymerization, targeting of the formin mDia did [Butler et al., 2006].

Butler, B., Gao, C., Mersich, A. T. and Blystone, S. D. (2006). Purified integrin adhesion complexes exhibit actin-polymerization activity. Curr. Biol. 16, 242-251.

DeMali, K. A., Barlow, C. A. and Burridge, K. (2002). Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J. Cell Biol. 159, 881-891.

Galbraith, C. G., Yamada, K. M. and Galbraith, J. A. (2007). Polymerizing actin fibers position integrins primed to probe for adhesion sites. Science 315, 992-995.

Kiosses, W. B., Shattil, S. J., Pampori, N. and Schwartz, M. A. (2001). Rac recruits high-affinity integrin alphavbeta3 to lamellipodia in endothelial cell migration. Nat. Cell Biol. 3, 316-320.

Serrels, B., Serrels, A., Brunton, V. G., Holt, M., McLean, G. W., Gray, C. H., Jones, G. E. and Frame, M. C. (2007). Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex. Nat. Cell Biol. 9, 1046-1056.

[Seite 201]

In this context, the direct interaction of focal adhesion kinase (FAK) and vinculin with the Arp2/3 complex (DeMali et al., 2002; Serrels et al., 2007), the main nucleator of actin branching and polymerization in lamellipodia, constitutes a possible mechanism for targeting vinculin and FAK to future adhesion sites. The presence of activated integrins in regions of protrusion outside adhesions suggests that they enter the forming adhesion in an activated state (Galbraith et al., 2007; Kiosses et al., 2001). The other implication is that adhesions might nucleate actin polymerization. This would provide a mechanism for the formation of actin filaments on which adhesions elongate; these appear to elongate from nascent adhesions at the lamellipodium-lamellum interface. This possibility is supported by the observation that purified integrin-adhesion complexes have actin-polymerization activity (Butler et al., 2006). Although the neutralization of Arp2/3 in

[Seite 202]

β3-integrin-containing adhesion complexes did not impair actin polymerization, targeting of the formin mDia did (Butler et al., 2006).


Butler, B., Gao, C., Mersich, A. T. and Blystone, S. D. (2006). Purified integrin adhesion complexes exhibit actin-polymerization activity. Curr. Biol. 16, 242-251.

DeMali, K. A., Barlow, C. A. and Burridge, K. (2002). Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J. Cell Biol. 159, 881-891.

Galbraith, C. G., Yamada, K. M. and Galbraith, J. A. (2007). Polymerizing actin fibers position integrins primed to probe for adhesion sites. Science 315, 992-995.

Kiosses, W. B., Shattil, S. J., Pampori, N. and Schwartz, M. A. (2001). Rac recruits high-affinity integrin alphavbeta3 to lamellipodia in endothelial cell migration. Nat. Cell Biol. 3, 316-320.

Serrels, B., Serrels, A., Brunton, V. G., Holt, M., McLean, G. W., Gray, C. H., Jones, G. E. and Frame, M. C. (2007). Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex. Nat. Cell Biol. 9, 1046-1056.

Anmerkungen

Art und Umfang der Übernahme bleiben ungekennzeichnet.

Sichter
(Graf Isolan), SleepyHollow02

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