Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo

BilanciaC.G.; WinkelmanJ.D.; TsygankovD.; NowotarskiS.H.; SeesJ.A.; ComberK.; EvansI.; LakhaniV.; WoodW.; ElstonT.C.; KovarD.R.; PeiferM.

首页> 外文期刊>Developmental cell >Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo

【24h】

Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo

机译：启用在体外和体内负面调节透色驱动的肌动蛋白动力学

获取原文

获取原文并翻译 | 示例

获取外文期刊封面封底 >>

开具论文收录证明 >>

文献代查 >>

页面导航

摘要
著录项
相似文献
相关主题

摘要

Actin regulators facilitate cell migration by controlling cell protrusion architecture and dynamics. As the behavior of individual actin regulators becomes clear, we must address why cells require multiple regulators with similar functions and how they cooperate to create diverse protrusions. We characterized Diaphanous (Dia) and Enabled (Ena) as a model, using complementary approaches: cell culture, biophysical analysis, and Drosophila morphogenesis. We found that Dia and Ena have distinct biochemical properties that contribute to the different protrusion morphologies each induces. Dia is a more processive, faster elongator, paralleling the long, stable filopodia it induces invivo, while Ena promotes filopodia with more dynamic changes in number, length, and lifetime. Acting together, Ena and Dia induce protrusions distinct from those induced by either alone, with Ena reducing Dia-driven protrusion length and number. Consistent with this, EnaEVH1 binds Dia directly and inhibits DiaFH1FH2-mediated nucleation invitro. Finally, Ena rescues hemocyte migration defects caused by activated Dia.

机译：肌动蛋白调节剂通过控制细胞突起结构和动力学促进细胞迁移。随着各个肌动蛋白调节剂的行为变得清晰，我们必须解决为什么细胞需要具有相似功能的多个调节剂，以及它们如何协同作用以形成多种突起。我们使用补充方法：细胞培养，生物物理分析和果蝇形态发生，将透照（Dia）和使能（Ena）表征为模型。我们发现，Dia和Ena具有不同的生化特性，它们分别促成不同的突起形态。 Dia是一种更具发展力的，更快的伸长剂，与长而稳定的丝状伪足平行，它诱导了体内存活，而Ena则通过数量，长度和寿命的更多动态变化来促进丝状伪足。 Ena和Dia共同作用，会产生不同于单独使用的突起，而Ena会减少Dia驱动的突起长度和数量。与此一致，EnaEVH1直接与Dia结合并抑制DiaFH1FH2介导的体外成核。最后，Ena挽救了由激活的Dia引起的血细胞迁移缺陷。

著录项

来源
《Developmental cell》 |2014年第4期|共15页
作者
BilanciaC.G.; WinkelmanJ.D.; TsygankovD.; NowotarskiS.H.; SeesJ.A.; ComberK.; EvansI.; LakhaniV.; WoodW.; ElstonT.C.; KovarD.R.; PeiferM.;
展开▼
作者单位

展开▼
收录信息
原文格式 PDF
正文语种 eng
中图分类细胞生物学;
关键词

相似文献

外文文献
中文文献
专利

1. Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo [J] . BilanciaC.G., WinkelmanJ.D., TsygankovD., Developmental cell . 2014,第4期

机译：启用在体外和体内负面调节透色驱动的肌动蛋白动力学
2. Lasp-1 binds to non-muscle F-actin in vitro and is localized within multiple sites of dynamic actin assembly in vivo. [J] . Chew CS, Chen X, Parente JA Jr, Journal of Cell Science . 2002,第Pta24期

机译：Lasp-1在体外与非肌肉F-肌动蛋白结合，并在体内位于动态肌动蛋白装配的多个位点内。
3. Lasp-1 binds to non-muscle F-actin in vitro and is localized within multiple sites of dynamic actin assembly in vivo [J] . Chew CS., Chen XS., Parente JA., Journal of Cell Science . 2002,第24期

机译：Lasp-1在体外与非肌肉F-肌动蛋白结合，并在体内位于动态肌动蛋白装配的多个位点
4. Altering hydrogel crosslinking structure to control mechanics and regulate microvessel formation in vitro and in vivo [C] . Ryan Schweller, Bruce Klitzman, Jennifer L West World biomaterials congress . 2016

机译：改变水凝胶的交联结构，以在体外和体内控制力学并调节微血管的形成
5. Mathematical modeling and analysis of in vitro actin filament dynamics and cell blebbing. [D] . Hu, Jifeng. 2009

机译：体外肌动蛋白丝动力学和细胞起泡的数学建模和分析。
6. Enabled Negatively Regulates Diaphanous-Driven Actin Dynamics In Vitro and In Vivo [O] . Colleen G. Bilancia, Jonathan D. Winkelman, Denis Tsygankov, -1

机译：启用负面地调节体外和体内的透明驱动肌动蛋白动力学
7. Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo [O] . Bilancia, Colleen G., Winkelman, Jonathan D., Tsygankov, Denis, 2014

机译：启用在体外和体内负面调节透色驱动的肌动蛋白动力学
8. Actin Filament Alterations in Rat Hepatocytes Induced In vivo and In vitro byMicrocystin-LR, a Hepatotoxin from the Blue-Green Alga, Microcystis aeruginosa [R] . Hooser, S. B., Beasley, V. R., Waite, L. L., 1991

机译：体外和体外诱导大鼠肝细胞肌动蛋白丝改变的微囊藻毒素-L，一种来自蓝绿藻的铜毒素，铜绿微囊藻

Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo

摘要

著录项

相似文献

相关主题

期刊订阅