Home > Publications database > One step ahead: Role of filopodia in adhesion formation during cell migration of keratinocytes > print |
001 | 4909 | ||
005 | 20200402205620.0 | ||
024 | 7 | _ | |2 pmid |a pmid:19100734 |
024 | 7 | _ | |2 DOI |a 10.1016/j.yexcr.2008.11.008 |
024 | 7 | _ | |2 WOS |a WOS:000265126900012 |
037 | _ | _ | |a PreJuSER-4909 |
041 | _ | _ | |a eng |
082 | _ | _ | |a 570 |
084 | _ | _ | |2 WoS |a Oncology |
084 | _ | _ | |2 WoS |a Cell Biology |
100 | 1 | _ | |a Schäfer, C. |b 0 |u FZJ |0 P:(DE-Juel1)VDB8500 |
245 | _ | _ | |a One step ahead: Role of filopodia in adhesion formation during cell migration of keratinocytes |
260 | _ | _ | |a Orlando, Fla. |b Academic Press |c 2009 |
300 | _ | _ | |a 1212 - 1224 |
336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
336 | 7 | _ | |a ARTICLE |2 BibTeX |
336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
336 | 7 | _ | |a article |2 DRIVER |
440 | _ | 0 | |a Experimental Cell Research |x 0014-4827 |0 13781 |y 7 |v 315 |
500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
520 | _ | _ | |a Cell 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. |
536 | _ | _ | |a Kondensierte Materie |c P54 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK414 |x 0 |
588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
650 | _ | 2 | |2 MeSH |a Cell Adhesion: physiology |
650 | _ | 2 | |2 MeSH |a Cell Adhesion Molecules: metabolism |
650 | _ | 2 | |2 MeSH |a Cell Movement: physiology |
650 | _ | 2 | |2 MeSH |a Cells, Cultured |
650 | _ | 2 | |2 MeSH |a Cytoskeletal Proteins: genetics |
650 | _ | 2 | |2 MeSH |a Cytoskeletal Proteins: metabolism |
650 | _ | 2 | |2 MeSH |a Fluorescence Recovery After Photobleaching |
650 | _ | 2 | |2 MeSH |a Focal Adhesions: metabolism |
650 | _ | 2 | |2 MeSH |a Glycoproteins: genetics |
650 | _ | 2 | |2 MeSH |a Glycoproteins: metabolism |
650 | _ | 2 | |2 MeSH |a Humans |
650 | _ | 2 | |2 MeSH |a Keratinocytes: cytology |
650 | _ | 2 | |2 MeSH |a Keratinocytes: physiology |
650 | _ | 2 | |2 MeSH |a Microfilament Proteins: metabolism |
650 | _ | 2 | |2 MeSH |a Paxillin: genetics |
650 | _ | 2 | |2 MeSH |a Paxillin: metabolism |
650 | _ | 2 | |2 MeSH |a Phosphoproteins: metabolism |
650 | _ | 2 | |2 MeSH |a Pseudopodia: metabolism |
650 | _ | 2 | |2 MeSH |a Pseudopodia: ultrastructure |
650 | _ | 2 | |2 MeSH |a Recombinant Fusion Proteins: genetics |
650 | _ | 2 | |2 MeSH |a Recombinant Fusion Proteins: metabolism |
650 | _ | 2 | |2 MeSH |a Talin: genetics |
650 | _ | 2 | |2 MeSH |a Talin: metabolism |
650 | _ | 2 | |2 MeSH |a Vinculin: genetics |
650 | _ | 2 | |2 MeSH |a Vinculin: metabolism |
650 | _ | 2 | |2 MeSH |a Zyxin |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a Cell Adhesion Molecules |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a Cytoskeletal Proteins |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a Glycoproteins |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a Microfilament Proteins |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a Paxillin |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a Phosphoproteins |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a Recombinant Fusion Proteins |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a Talin |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a ZYX protein, human |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a Zyxin |
650 | _ | 7 | |0 0 |2 NLM Chemicals |a vasodilator-stimulated phosphoprotein |
650 | _ | 7 | |0 125361-02-6 |2 NLM Chemicals |a Vinculin |
650 | _ | 7 | |a J |2 WoSType |
653 | 2 | 0 | |2 Author |a Filopodium |
653 | 2 | 0 | |2 Author |a Cell migration |
653 | 2 | 0 | |2 Author |a VASP |
653 | 2 | 0 | |2 Author |a Cell adhesion |
653 | 2 | 0 | |2 Author |a Focal adhesion |
653 | 2 | 0 | |2 Author |a Tip complex |
653 | 2 | 0 | |2 Author |a Keratinocytes |
653 | 2 | 0 | |2 Author |a Actin |
653 | 2 | 0 | |2 Author |a Fascin |
700 | 1 | _ | |a Borm, B. |b 1 |0 P:(DE-HGF)0 |
700 | 1 | _ | |a Born, S. |b 2 |u FZJ |0 P:(DE-Juel1)161241 |
700 | 1 | _ | |a Möhl, C. |b 3 |u FZJ |0 P:(DE-Juel1)VDB71075 |
700 | 1 | _ | |a Eibl, E.M. |b 4 |u FZJ |0 P:(DE-Juel1)VDB84707 |
700 | 1 | _ | |a Hoffmann, B. |b 5 |u FZJ |0 P:(DE-Juel1)VDB27696 |
773 | _ | _ | |a 10.1016/j.yexcr.2008.11.008 |g Vol. 315, p. 1212 - 1224 |p 1212 - 1224 |q 315<1212 - 1224 |0 PERI:(DE-600)1466780-0 |t Experimental cell research |v 315 |y 2009 |x 0014-4827 |
856 | 7 | _ | |u http://dx.doi.org/10.1016/j.yexcr.2008.11.008 |
909 | C | O | |o oai:juser.fz-juelich.de:4909 |p VDB |
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915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
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