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000004909 0247_ $$2pmid$$apmid:19100734
000004909 0247_ $$2DOI$$a10.1016/j.yexcr.2008.11.008
000004909 0247_ $$2WOS$$aWOS:000265126900012
000004909 037__ $$aPreJuSER-4909
000004909 041__ $$aeng
000004909 082__ $$a570
000004909 084__ $$2WoS$$aOncology
000004909 084__ $$2WoS$$aCell Biology
000004909 1001_ $$0P:(DE-Juel1)VDB8500$$aSchäfer, C.$$b0$$uFZJ
000004909 245__ $$aOne step ahead: Role of filopodia in adhesion formation during cell migration of keratinocytes
000004909 260__ $$aOrlando, Fla.$$bAcademic Press$$c2009
000004909 300__ $$a1212 - 1224
000004909 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000004909 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000004909 3367_ $$2DRIVER$$aarticle
000004909 440_0 $$013781$$aExperimental Cell Research$$v315$$x0014-4827$$y7
000004909 500__ $$aRecord converted from VDB: 12.11.2012
000004909 520__ $$aCell adhesion is an essential prerequisite for cell function and movement. It depends strongly on focal adhesion complexes connecting the extracellular matrix to the actin cytoskeleton. Especially in moving cells focal adhesions are highly dynamic and believed to be formed closely behind the leading edge. Filopodia were thought to act mainly as guiding cues using their tip complexes for elongation. Here we show for keratinocytes a strong dependence of lamellipodial adhesion sites on filopodia. Upon stable contact of the VASP-containing tip spot to the substrate, a filopodial focal complex (filopodial FX) is formed right behind along the filopodia axis. These filopodial FXs are fully assembled, yet small adhesions containing all adhesion markers tested. Filopodial FXs when reached by the lamellipodium are just increased in size resulting in classical focal adhesions. At the same time most filopodia regain their elongation ability. Blocking filopodia inhibits development of new focal adhesions in the lamellipodium, while focal adhesion maturation in terms of vinculin exchange dynamics remains active. Our data therefore argue for a strong spatial and temporal dependence of focal adhesions on filopodial focal complexes in keratinocytes with filopodia not permanently initiated via new clustering of actin filaments to induce elongation.
000004909 536__ $$0G:(DE-Juel1)FUEK414$$2G:(DE-HGF)$$aKondensierte Materie$$cP54$$x0
000004909 588__ $$aDataset connected to Web of Science, Pubmed
000004909 650_2 $$2MeSH$$aCell Adhesion: physiology
000004909 650_2 $$2MeSH$$aCell Adhesion Molecules: metabolism
000004909 650_2 $$2MeSH$$aCell Movement: physiology
000004909 650_2 $$2MeSH$$aCells, Cultured
000004909 650_2 $$2MeSH$$aCytoskeletal Proteins: genetics
000004909 650_2 $$2MeSH$$aCytoskeletal Proteins: metabolism
000004909 650_2 $$2MeSH$$aFluorescence Recovery After Photobleaching
000004909 650_2 $$2MeSH$$aFocal Adhesions: metabolism
000004909 650_2 $$2MeSH$$aGlycoproteins: genetics
000004909 650_2 $$2MeSH$$aGlycoproteins: metabolism
000004909 650_2 $$2MeSH$$aHumans
000004909 650_2 $$2MeSH$$aKeratinocytes: cytology
000004909 650_2 $$2MeSH$$aKeratinocytes: physiology
000004909 650_2 $$2MeSH$$aMicrofilament Proteins: metabolism
000004909 650_2 $$2MeSH$$aPaxillin: genetics
000004909 650_2 $$2MeSH$$aPaxillin: metabolism
000004909 650_2 $$2MeSH$$aPhosphoproteins: metabolism
000004909 650_2 $$2MeSH$$aPseudopodia: metabolism
000004909 650_2 $$2MeSH$$aPseudopodia: ultrastructure
000004909 650_2 $$2MeSH$$aRecombinant Fusion Proteins: genetics
000004909 650_2 $$2MeSH$$aRecombinant Fusion Proteins: metabolism
000004909 650_2 $$2MeSH$$aTalin: genetics
000004909 650_2 $$2MeSH$$aTalin: metabolism
000004909 650_2 $$2MeSH$$aVinculin: genetics
000004909 650_2 $$2MeSH$$aVinculin: metabolism
000004909 650_2 $$2MeSH$$aZyxin
000004909 650_7 $$00$$2NLM Chemicals$$aCell Adhesion Molecules
000004909 650_7 $$00$$2NLM Chemicals$$aCytoskeletal Proteins
000004909 650_7 $$00$$2NLM Chemicals$$aGlycoproteins
000004909 650_7 $$00$$2NLM Chemicals$$aMicrofilament Proteins
000004909 650_7 $$00$$2NLM Chemicals$$aPaxillin
000004909 650_7 $$00$$2NLM Chemicals$$aPhosphoproteins
000004909 650_7 $$00$$2NLM Chemicals$$aRecombinant Fusion Proteins
000004909 650_7 $$00$$2NLM Chemicals$$aTalin
000004909 650_7 $$00$$2NLM Chemicals$$aZYX protein, human
000004909 650_7 $$00$$2NLM Chemicals$$aZyxin
000004909 650_7 $$00$$2NLM Chemicals$$avasodilator-stimulated phosphoprotein
000004909 650_7 $$0125361-02-6$$2NLM Chemicals$$aVinculin
000004909 650_7 $$2WoSType$$aJ
000004909 65320 $$2Author$$aFilopodium
000004909 65320 $$2Author$$aCell migration
000004909 65320 $$2Author$$aVASP
000004909 65320 $$2Author$$aCell adhesion
000004909 65320 $$2Author$$aFocal adhesion
000004909 65320 $$2Author$$aTip complex
000004909 65320 $$2Author$$aKeratinocytes
000004909 65320 $$2Author$$aActin
000004909 65320 $$2Author$$aFascin
000004909 7001_ $$0P:(DE-HGF)0$$aBorm, B.$$b1
000004909 7001_ $$0P:(DE-Juel1)161241$$aBorn, S.$$b2$$uFZJ
000004909 7001_ $$0P:(DE-Juel1)VDB71075$$aMöhl, C.$$b3$$uFZJ
000004909 7001_ $$0P:(DE-Juel1)VDB84707$$aEibl, E.M.$$b4$$uFZJ
000004909 7001_ $$0P:(DE-Juel1)VDB27696$$aHoffmann, B.$$b5$$uFZJ
000004909 773__ $$0PERI:(DE-600)1466780-0$$a10.1016/j.yexcr.2008.11.008$$gVol. 315, p. 1212 - 1224$$p1212 - 1224$$q315<1212 - 1224$$tExperimental cell research$$v315$$x0014-4827$$y2009
000004909 8567_ $$uhttp://dx.doi.org/10.1016/j.yexcr.2008.11.008
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000004909 9131_ $$0G:(DE-Juel1)FUEK414$$bMaterie$$kP54$$lKondensierte Materie$$vKondensierte Materie$$x0$$zentfällt   bis 2009
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000004909 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000004909 9201_ $$0I:(DE-Juel1)VDB802$$d31.12.2010$$gIBN$$kIBN-4$$lBiomechanik$$x0
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