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@ARTICLE{Schfer:10585,
author = {Schäfer, C. and Born, S. and Möhl, C. and Houben, S. and
Kirchgeßner, N. and Merkel, R. and Hoffmann, B.},
title = {{T}he key feature for early migratory processes:
{D}ependence of adhesion actin bundles, force generation and
transmission of filopodia},
journal = {Cell adhesion $\&$ migration},
volume = {4},
issn = {1933-6918},
address = {Austin, Tex.},
publisher = {Landes Bioscience},
reportid = {PreJuSER-10585},
pages = {215 - 225},
year = {2010},
note = {Record converted from VDB: 12.11.2012},
abstract = {Migration of cells is one of the most essential
prerequisites to form higher organisms and depends on a
strongly coordinated sequence of processes. Early migratory
events include substrate sensing, adhesion formation, actin
bundle assembly and force generation. While substrate
sensing was ascribed to filopodia, all other processes were
believed to depend mainly on lamellipodia of migrating
cells. In this work we show for motile keratinocytes that
all processes from substrate sensing to force generation
strongly depend on filopodial focal complexes as well as on
filopodial actin bundles. In a coordinated step by step
process, filopodial focal complexes have to be tightly
adhered to the substrate and to filopodial actin bundles to
enlarge upon lamellipodial contact forming classical focal
adhesions. Lamellipodial actin filaments attached to those
focal adhesions originate from filopodia. Upon cell
progression, the incorporation of filopodial actin bundles
into the lamellipodium goes along with a complete change in
actin cross-linker composition from filopodial fascin to
lamellipodial alpha-actinin. alpha-Actinin in turn is
replaced by myosin II and becomes incorporated directly
behind the leading edge. Myosin II activity makes this class
of actin bundles with their attached FAs the major source of
force generation and transmission at the cell front.
Furthermore, connection of FAs to force generating actin
bundles leads to their stabilization and further
enlargement. Consequently, adhesion sites formed
independently of filopodia are not connected to detectable
actin bundles, transmit weak forces to the substrate and
disassemble within a few minutes without having been
increased in size.},
keywords = {J (WoSType)},
cin = {IBN-4},
ddc = {570},
cid = {I:(DE-Juel1)VDB802},
pnm = {BioSoft: Makromolekulare Systeme und biologische
Informationsverarbeitung},
pid = {G:(DE-Juel1)FUEK505},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000208234700014},
doi = {10.4161/cam.4.2.10745},
url = {https://juser.fz-juelich.de/record/10585},
}