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000141611 0247_ $$2doi$$a10.1016/j.cub.2019.09.040
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000141611 0247_ $$2ISSN$$a0960-9822
000141611 0247_ $$2ISSN$$a1879-0445
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000141611 037__ $$aDZNE-2020-07935
000141611 041__ $$aEnglish
000141611 082__ $$a570
000141611 1001_ $$0P:(DE-2719)2810386$$aDupraz, Sebastian$$b0$$udzne
000141611 245__ $$aRhoA Controls Axon Extension Independent of Specification in the Developing Brain.
000141611 260__ $$aLondon$$bCurrent Biology Ltd.$$c2019
000141611 264_1 $$2Crossref$$3print$$bElsevier BV$$c2019-11-01
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000141611 520__ $$aThe specification of an axon and its subsequent outgrowth are key steps during neuronal polarization, a prerequisite to wire the brain. The Rho-guanosine triphosphatase (GTPase) RhoA is believed to be a central player in these processes. However, its physiological role has remained undefined. Here, genetic loss- and gain-of-function experiments combined with time-lapse microscopy, cell culture, and in vivo analysis show that RhoA is not involved in axon specification but confines the initiation of neuronal polarization and axon outgrowth during development. Biochemical analysis and super-resolution microscopy together with molecular and pharmacological manipulations reveal that RhoA restrains axon growth by activating myosin-II-mediated actin arc formation in the growth cone to prevent microtubules from protruding toward the leading edge. Through this mechanism, RhoA regulates the duration of axon growth and pause phases, thus controlling the tightly timed extension of developing axons. Thereby, this work unravels physiologically relevant players coordinating actin-microtubule interactions during axon growth.
000141611 536__ $$0G:(DE-HGF)POF3-341$$a341 - Molecular Signaling (POF3-341)$$cPOF3-341$$fPOF III$$x0
000141611 542__ $$2Crossref$$i2019-11-01$$uhttps://www.elsevier.com/tdm/userlicense/1.0/
000141611 542__ $$2Crossref$$i2019-09-19$$uhttp://creativecommons.org/licenses/by-nc-nd/4.0/
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000141611 650_2 $$2MeSH$$aActin Cytoskeleton: metabolism
000141611 650_2 $$2MeSH$$aActins: metabolism
000141611 650_2 $$2MeSH$$aAnimals
000141611 650_2 $$2MeSH$$aAxons: metabolism
000141611 650_2 $$2MeSH$$aAxons: physiology
000141611 650_2 $$2MeSH$$aBrain: embryology
000141611 650_2 $$2MeSH$$aBrain: metabolism
000141611 650_2 $$2MeSH$$aCell Polarity: physiology
000141611 650_2 $$2MeSH$$aFemale
000141611 650_2 $$2MeSH$$aGain of Function Mutation: genetics
000141611 650_2 $$2MeSH$$aGrowth Cones: metabolism
000141611 650_2 $$2MeSH$$aLoss of Function Mutation: genetics
000141611 650_2 $$2MeSH$$aMale
000141611 650_2 $$2MeSH$$aMice
000141611 650_2 $$2MeSH$$aMice, Inbred C57BL
000141611 650_2 $$2MeSH$$aMice, Transgenic
000141611 650_2 $$2MeSH$$aMicrotubules: metabolism
000141611 650_2 $$2MeSH$$aMyosin Type II: metabolism
000141611 650_2 $$2MeSH$$aNeurogenesis: physiology
000141611 650_2 $$2MeSH$$aNeurons: metabolism
000141611 650_2 $$2MeSH$$arhoA GTP-Binding Protein: genetics
000141611 650_2 $$2MeSH$$arhoA GTP-Binding Protein: metabolism
000141611 650_2 $$2MeSH$$arhoA GTP-Binding Protein: physiology
000141611 7001_ $$0P:(DE-2719)2812271$$aHilton, Brett J$$b1$$udzne
000141611 7001_ $$0P:(DE-2719)2811971$$aHusch, Andreas$$b2$$udzne
000141611 7001_ $$0P:(DE-2719)2810952$$aDa Silva Santos, Telma$$b3$$udzne
000141611 7001_ $$0P:(DE-2719)2810781$$aColes, Charlotte H$$b4$$udzne
000141611 7001_ $$0P:(DE-2719)2810277$$aStern, Sina$$b5$$udzne
000141611 7001_ $$aBrakebusch, Cord$$b6
000141611 7001_ $$0P:(DE-2719)2810270$$aBradke, Frank$$b7$$eFirst author$$udzne
000141611 77318 $$2Crossref$$3journal-article$$a10.1016/j.cub.2019.09.040$$b : Elsevier BV, 2019-11-01$$n22$$p3874-3886.e9$$tCurrent Biology$$v29$$x0960-9822$$y2019
000141611 773__ $$0PERI:(DE-600)2019214-9$$a10.1016/j.cub.2019.09.040$$gVol. 29, no. 22, p. 3874 - 3886.e9$$n22$$p3874-3886.e9$$q29:22<3874 - 3886.e9$$tCurrent biology$$v29$$x0960-9822$$y2019
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