Structural and temporal requirements of Wnt/PCP protein Vangl2 function for convergence and extension movements and facial branchiomotor neuron migration in zebrafish.
Structural and temporal requirements of Wnt/PCP protein Vangl2 function for convergence and extension movements and facial branchiomotor neuron migration in zebrafish.
复制标题
Wnt/PCP 蛋白 Vangl2 功能对斑马鱼会聚和伸展运动以及面部鳃运动神经元迁移的结构和时间要求。
DOI：
10.1016/j.mod.2013.12.001
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发表时间：
2014
影响因子：
2.6
通讯作者：
Chandrasekhar,Anand
中科院分区：
文献类型：
--
作者：
Pan,Xiufang;Sittaramane,Vinoth;Gurung,Suman;Chandrasekhar,Anand
梵高样蛋白2(van Gogh-like 2，Vangl2)是Wnt/Plane cell Polity(PCP)信号通路的核心成分，是一种具有N-末端和C-末端结构域的四通道跨膜蛋白，在果蝇和哺乳动物中结构保守。在脊椎动物中，Vangl2在原肠发育过程中的会聚和伸展(CE)运动以及面支运动(FBM)神经元在后脑的迁移中起着至关重要的作用。然而，特定的Vangl2结构域、膜结合以及特定的细胞外和细胞内基序的作用还没有被研究，特别是在FBM神经元迁移的背景下。通过热休克诱导多种Vangl2转基因基因的表达，我们发现Vangl2的N端和C端结构域的膜相关功能参与调控FBM神经元的迁移。重要的是，通过温度漂移实验，我们发现Vangl2功能的关键期与FBM神经元从菱形核4迁移出来的初始阶段相吻合。有趣的是，我们还在C-末端区域发现了一个可能在调节CE运动中发挥作用的核定位基序。
Van gogh-like 2 (Vangl2), a core component of the Wnt/planar cell polarity (PCP) signaling pathway, is a four-pass transmembrane protein with N-terminal and C-terminal domains located in the cytosol, and is structurally conserved from flies to mammals. In vertebrates, Vangl2 plays an essential role in convergence and extension (CE) movements during gastrulation and in facial branchiomotor (FBM) neuron migration in the hindbrain. However, the roles of specific Vangl2 domains, of membrane association, and of specific extracellular and intracellular motifs have not been examined, especially in the context of FBM neuron migration. Through heat shock-inducible expression of various Vangl2 transgenes, we found that membrane associated functions of the N-terminal and C-terminal domains of Vangl2 are involved in regulating FBM neuron migration. Importantly, through temperature shift experiments, we found that the critical period for Vangl2 function coincides with the initial stages of FBM neuron migration out of rhombomere 4. Intriguingly, we have also uncovered a putative nuclear localization motif in the C-terminal domain that may play a role in regulating CE movements.