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000010585 0247_ $$2DOI$$a10.4161/cam.4.2.10745
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000010585 1001_ $$0P:(DE-Juel1)VDB8500$$aSchäfer, C.$$b0$$uFZJ
000010585 245__ $$aThe key feature for early migratory processes: Dependence of adhesion actin bundles, force generation and transmission of filopodia
000010585 260__ $$aAustin, Tex.$$bLandes Bioscience$$c2010
000010585 300__ $$a215 - 225
000010585 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000010585 440_0 $$023405$$aCell Adhesion and Migration$$v4$$x1933-6918$$y2
000010585 500__ $$aRecord converted from VDB: 12.11.2012
000010585 520__ $$aMigration of cells is one of the most essential prerequisites to form higher organisms and depends on a strongly coordinated sequence of processes. Early migratory events include substrate sensing, adhesion formation, actin bundle assembly and force generation. While substrate sensing was ascribed to filopodia, all other processes were believed to depend mainly on lamellipodia of migrating cells. In this work we show for motile keratinocytes that all processes from substrate sensing to force generation strongly depend on filopodial focal complexes as well as on filopodial actin bundles. In a coordinated step by step process, filopodial focal complexes have to be tightly adhered to the substrate and to filopodial actin bundles to enlarge upon lamellipodial contact forming classical focal adhesions. Lamellipodial actin filaments attached to those focal adhesions originate from filopodia. Upon cell progression, the incorporation of filopodial actin bundles into the lamellipodium goes along with a complete change in actin cross-linker composition from filopodial fascin to lamellipodial alpha-actinin. alpha-Actinin in turn is replaced by myosin II and becomes incorporated directly behind the leading edge. Myosin II activity makes this class of actin bundles with their attached FAs the major source of force generation and transmission at the cell front. Furthermore, connection of FAs to force generating actin bundles leads to their stabilization and further enlargement. Consequently, adhesion sites formed independently of filopodia are not connected to detectable actin bundles, transmit weak forces to the substrate and disassemble within a few minutes without having been increased in size.
000010585 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x0
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000010585 65320 $$2Author$$afilopodia
000010585 65320 $$2Author$$afocal complexes
000010585 65320 $$2Author$$acell migration
000010585 65320 $$2Author$$afocal adhesion
000010585 65320 $$2Author$$amyosin II
000010585 65320 $$2Author$$aforce
000010585 65320 $$2Author$$aactin flow
000010585 65320 $$2Author$$amaturation
000010585 650_7 $$2WoSType$$aJ
000010585 7001_ $$0P:(DE-Juel1)161241$$aBorn, S.$$b1$$uFZJ
000010585 7001_ $$0P:(DE-Juel1)VDB71075$$aMöhl, C.$$b2$$uFZJ
000010585 7001_ $$0P:(DE-Juel1)VDB87855$$aHouben, S.$$b3$$uFZJ
000010585 7001_ $$0P:(DE-Juel1)VDB8902$$aKirchgeßner, N.$$b4$$uFZJ
000010585 7001_ $$0P:(DE-Juel1)128833$$aMerkel, R.$$b5$$uFZJ
000010585 7001_ $$0P:(DE-Juel1)VDB27696$$aHoffmann, B.$$b6$$uFZJ
000010585 773__ $$0PERI:(DE-600)2268518-2$$a10.4161/cam.4.2.10745$$gVol. 4, p. 215 - 225$$p215 - 225$$q4<215 - 225$$tCell adhesion & migration$$v4$$x1933-6918$$y2010
000010585 8567_ $$uhttp://dx.doi.org/10.4161/cam.4.2.10745
000010585 909CO $$ooai:juser.fz-juelich.de:10585$$pVDB
000010585 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000010585 915__ $$0StatID:(DE-HGF)0020$$aNo peer review
000010585 9141_ $$y2010
000010585 9131_ $$0G:(DE-Juel1)FUEK505$$bSchlüsseltechnologien$$kP45$$lBiologische Informationsverarbeitung$$vBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$x0
000010585 9132_ $$0G:(DE-HGF)POF3-552$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$aDE-HGF$$bKey Technologies$$lBioSoft  Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vEngineering Cell Function$$x0
000010585 9201_ $$0I:(DE-Juel1)VDB802$$d31.12.2010$$gIBN$$kIBN-4$$lBiomechanik$$x0
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