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dc.contributor.authorFaix, Jan
dc.contributor.authorBreitsprecher, Dennis
dc.contributor.authorStradal, Theresia E B
dc.contributor.authorRottner, Klemens
dc.date.accessioned2009-08-12T13:07:50Z
dc.date.available2009-08-12T13:07:50Z
dc.date.issued2009-08-12T13:07:50Z
dc.identifier.citationFilopodia: Complex models for simple rods., 41 (8-9):1656-64 Int. J. Biochem. Cell Biol.en
dc.identifier.issn1878-5875
dc.identifier.pmid19433307
dc.identifier.doi10.1016/j.biocel.2009.02.012
dc.identifier.urihttp://hdl.handle.net/10033/77073
dc.description.abstractFilopodia are prominent cell surface projections filled with bundles of linear actin filaments that drive their protrusion. These structures are considered important sensory organelles, for instance in neuronal growth cones or during the fusion of sheets of epithelial tissues. In addition, they can serve a precursor function in adhesion site or stress fibre formation. Actin filament assembly is essential for filopodia formation and turnover, yet the precise molecular mechanisms of filament nucleation and/or elongation are controversial. Indeed, conflicting reports on the molecular requirements of filopodia initiation have prompted researchers to propose different types and/or alternative or redundant mechanisms mediating this process. However, recent data shed new light on these questions, and they indicate that the balance of a limited set of biochemical activities can determine the structural outcome of a given filopodium. Here we focus on discussing our current view of the relevance of these activities, and attempt to propose a molecular mechanism of filopodia assembly based on a single core machinery.
dc.language.isoenen
dc.subject.meshAnimalsen
dc.subject.meshCytoskeletal Proteinsen
dc.subject.meshHumansen
dc.subject.meshMicrofilamentsen
dc.subject.meshModels, Biologicalen
dc.subject.meshNerve Tissue Proteinsen
dc.subject.meshPseudopodiaen
dc.subject.meshrho GTP-Binding Proteinsen
dc.titleFilopodia: Complex models for simple rods.en
dc.typeArticleen
dc.contributor.departmentInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany. faix@bpc.mh-hannover.deen
dc.identifier.journalThe international journal of biochemistry & cell biologyen
refterms.dateFOA2018-06-13T09:22:47Z
html.description.abstractFilopodia are prominent cell surface projections filled with bundles of linear actin filaments that drive their protrusion. These structures are considered important sensory organelles, for instance in neuronal growth cones or during the fusion of sheets of epithelial tissues. In addition, they can serve a precursor function in adhesion site or stress fibre formation. Actin filament assembly is essential for filopodia formation and turnover, yet the precise molecular mechanisms of filament nucleation and/or elongation are controversial. Indeed, conflicting reports on the molecular requirements of filopodia initiation have prompted researchers to propose different types and/or alternative or redundant mechanisms mediating this process. However, recent data shed new light on these questions, and they indicate that the balance of a limited set of biochemical activities can determine the structural outcome of a given filopodium. Here we focus on discussing our current view of the relevance of these activities, and attempt to propose a molecular mechanism of filopodia assembly based on a single core machinery.


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