TY  - JOUR
AU  - Schäfer, C.
AU  - Borm, B.
AU  - Born, S.
AU  - Möhl, C.
AU  - Eibl, E.M.
AU  - Hoffmann, B.
TI  - One step ahead: Role of filopodia in adhesion formation during cell migration of keratinocytes
JO  - Experimental cell research
VL  - 315
SN  - 0014-4827
CY  - Orlando, Fla.
PB  - Academic Press
M1  - PreJuSER-4909
SP  - 1212 - 1224
PY  - 2009
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - Cell Adhesion: physiology
KW  - Cell Adhesion Molecules: metabolism
KW  - Cell Movement: physiology
KW  - Cells, Cultured
KW  - Cytoskeletal Proteins: genetics
KW  - Cytoskeletal Proteins: metabolism
KW  - Fluorescence Recovery After Photobleaching
KW  - Focal Adhesions: metabolism
KW  - Glycoproteins: genetics
KW  - Glycoproteins: metabolism
KW  - Humans
KW  - Keratinocytes: cytology
KW  - Keratinocytes: physiology
KW  - Microfilament Proteins: metabolism
KW  - Paxillin: genetics
KW  - Paxillin: metabolism
KW  - Phosphoproteins: metabolism
KW  - Pseudopodia: metabolism
KW  - Pseudopodia: ultrastructure
KW  - Recombinant Fusion Proteins: genetics
KW  - Recombinant Fusion Proteins: metabolism
KW  - Talin: genetics
KW  - Talin: metabolism
KW  - Vinculin: genetics
KW  - Vinculin: metabolism
KW  - Zyxin
KW  - Cell Adhesion Molecules (NLM Chemicals)
KW  - Cytoskeletal Proteins (NLM Chemicals)
KW  - Glycoproteins (NLM Chemicals)
KW  - Microfilament Proteins (NLM Chemicals)
KW  - Paxillin (NLM Chemicals)
KW  - Phosphoproteins (NLM Chemicals)
KW  - Recombinant Fusion Proteins (NLM Chemicals)
KW  - Talin (NLM Chemicals)
KW  - ZYX protein, human (NLM Chemicals)
KW  - Zyxin (NLM Chemicals)
KW  - vasodilator-stimulated phosphoprotein (NLM Chemicals)
KW  - Vinculin (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:19100734
UR  - <Go to ISI:>//WOS:000265126900012
DO  - DOI:10.1016/j.yexcr.2008.11.008
UR  - https://juser.fz-juelich.de/record/4909
ER  -