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@ARTICLE{Schfer:21270,
author = {Schäfer, C. and Faust, U. and Kirchgeßner, N. and Merkel,
R. and Hoffmann, B.},
title = {{T}he {F}ilopodium: {A} stable structure with highly
regulated repetitive cycles of elongation and persistence},
journal = {Cell adhesion $\&$ migration},
volume = {5},
issn = {1933-6918},
address = {Austin, Tex.},
publisher = {Landes Bioscience},
reportid = {PreJuSER-21270},
pages = {431 - 438},
year = {2011},
note = {Record converted from VDB: 12.11.2012},
abstract = {The ability of mammalian cells to adhere and to migrate is
an essential prerequisite to form higher organisms. Early
migratory events include substrate sensing, adhesion
formation, actin bundle assembly and force generation.
Latest research revealed that filopodia are important not
only for sensing the substrate but for all of the
aforementioned highly regulated processes. However, the
exact regulatory mechanisms are still barely understood.
Here, we demonstrate that filopodia of human keratinocytes
exhibit distinct cycles of repetitive elongation and
persistence. A single filopodium thereby is able to initiate
the formation of several stable adhesions. Every single
filopodial cycle is characterized by an elongation phase,
followed by a stabilization time and in many cases a
persistence phase. The whole process is strongly connected
to the velocity of the lamellipodial leading edge,
characterized by a similar phase behavior with a slight time
shift compared to filopodia and a different velocity. Most
importantly, re-growth of existing filopodia is induced at a
sharply defined distance between the filopodial tip and the
lamellipodial leading edge. On the molecular level this
re-growth is preceded by a strong filopodial reduction of
the actin bundling protein fascin. This reduction is
achieved by a switch to actin polymerization without fascin
incorporation at the filopodial tip and therefore subsequent
out-transport of the cross-linker by actin retrograde flow.},
keywords = {Actins: chemistry / Actins: metabolism / Carrier Proteins:
metabolism / Cell Adhesion: physiology / Cell Adhesion
Molecules: chemistry / Cell Adhesion Molecules: metabolism /
Cell Line / Cell Movement / Focal Adhesions: metabolism /
Humans / Keratinocytes: cytology / Keratinocytes: metabolism
/ Microfilament Proteins: chemistry / Microfilament
Proteins: metabolism / Polymerization / Pseudopodia:
chemistry / Pseudopodia: metabolism / Actins (NLM Chemicals)
/ Carrier Proteins (NLM Chemicals) / Cell Adhesion Molecules
(NLM Chemicals) / Microfilament Proteins (NLM Chemicals) /
fascin (NLM Chemicals) / J (WoSType)},
cin = {ICS-7},
ddc = {570},
cid = {I:(DE-Juel1)ICS-7-20110106},
pnm = {BioSoft: Makromolekulare Systeme und biologische
Informationsverarbeitung},
pid = {G:(DE-Juel1)FUEK505},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:21975552},
pmc = {pmc:PMC3218610},
UT = {WOS:000300713700008},
doi = {10.4161/cam.5.5.17400},
url = {https://juser.fz-juelich.de/record/21270},
}