Misexpression of the catenin p120(ctn)1A perturbs Xenopus gastrulation but does not elicit Wnt-directed axis specification.

Misexpression of the catenin p120(ctn)1A perturbs Xenopus gastrulation but does not elicit Wnt-directed axis specification.
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连环蛋白 p120(ctn)1A 的错误表达会扰乱非洲爪蟾原肠胚形成,但不会引起 Wnt 定向轴规范。

DOI:
10.1006/dbio.1998.9158
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发表时间:
1999
影响因子:
2.7
通讯作者:
McCrea,PD
McCrea,PD
中科院分区:
生物学3区
文献类型:
--
作者:
Paulson,AF;Fang,X;Ji,H;Reynolds,AB;McCrea,PD

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钙粘蛋白功能的调节剂是非常感兴趣的,因为钙粘蛋白复合物积极地促进几乎所有组织的形态发生。连环蛋白p120 ctn(以前的p120 cas)首先被鉴定为src和受体蛋白酪氨酸激酶底物,后来被证明直接与钙粘蛋白相互作用。与β-catenin和斑珠蛋白(γ-catenin)一样,p120 ctn含有一个中央Armadillo重复区,通过该重复区结合钙粘蛋白胞质结构域。然而,很少有人知道p120 ctn在钙粘蛋白复合物中的功能。我们通过在非洲爪蟾中外源表达p120 ctn 1A来研究其在脊椎动物早期发育中的作用,与β-catenin相反,p120 ctn 1A的过表达并不诱导由Wnt信号通路激活引起的重复轴结构的形成,也不影响中胚层的诱导。相反,背侧p120的错误表达特异性地干扰原肠胚形成。对表达外源性p120 ctn的细胞的谱系追踪表明,细胞运动被破坏,而体外研究表明,这可能是卵裂球之间粘附减少的结果。因此,虽然钙粘蛋白结合蛋白β-连环蛋白、斑珠蛋白和p120 ctn是犰狳蛋白家族的成员,但很明显这些蛋白在早期脊椎动物发育中具有不同的生物学功能。这项工作表明,p120 ctn在钙粘蛋白的功能中发挥作用,p120 ctn的高表达干扰了形态发生所必需的适当的细胞-细胞相互作用。
Modulators of cadherin function are of great interest given that the cadherin complex actively contributes to the morphogenesis of virtually all tissues. The catenin p120ctn(formerly p120cas) was first identified as a src- and receptor-protein tyrosine kinase substrate and later shown to interact directly with cadherins. In common with β-catenin and plakoglobin (γ-catenin), p120ctncontains a central Armadillo repeat region by which it binds cadherin cytoplasmic domains. However, little is known about the function of p120ctnwithin the cadherin complex. We examined the role of p120ctn1A in early vertebrate development via its exogenous expression inXenopus.Ventral overexpression of p120ctn1A, in contrast to β-catenin, did not induce the formation of duplicate axial structures resulting from the activation of the Wnt signaling pathway, nor did p120ctnaffect mesoderm induction. Rather, dorsal misexpression of p120ctnspecifically perturbed gastrulation. Lineage tracing of cells expressing exogenous p120ctnindicated that cell movements were disrupted, whilein vitrostudies suggested that this may have been a consequence of reduced adhesion between blastomeres. Thus, while cadherin-binding proteins β-catenin, plakoglobin, and p120ctnare members of the Armadillo protein family, it is clear that these proteins have distinct biological functions in early vertebrate development. This work indicates that p120ctnhas a role in cadherin function and that heightened expression of p120ctninterferes with appropriate cell–cell interactions necessary for morphogenesis.