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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},
}