Epithelial tube morphogenesis during Drosophila tracheal development requires Piopio, a luminal ZP protein
Epithelial tube morphogenesis during Drosophila tracheal development requires Piopio, a luminal ZP protein
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DOI：
10.1038/ncb1049
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发表时间：
2003-10-01
影响因子：
21.3
通讯作者：
Affolter, M
中科院分区：
文献类型：
--
作者：
Jazwinska, A;Ribeiro, C;Affolter, M
分支上皮网络的形成是许多器官（如肺、肾或脉管系统）发育的基础。很少有人知道的机制，控制细胞重排在tubulogenesis和调节个别管的大小。最近的研究表明，而管细胞的基底表面与周围组织的相互作用，并有助于形成的分支模式的管状器官，顶端表面在管直径和管生长的调节中具有重要的作用。在这里，我们报告，两个蛋白质，Piopio（Pio）和Dumpy（Dp），含有一个透明质酸（ZP）结构域是必不可少的相互连接的气管网络在果蝇的产生。Pio从顶部分泌，积聚在气管腔中，并可能通过ZP结构域与Dp相互作用。在没有Pio和Dp的情况下，多细胞管不会通过细胞伸长和细胞插入重新排列以形成具有自体细胞连接的狭窄管;相反，它们被转化为多细胞囊肿，这导致分支模式的严重破坏。我们提出，含有Pio和Dp的细胞外基质在管腔空间中提供了一个结构网络，在该网络周围，细胞重排可以以有序的方式发生，而不会失去相互连接。我们的研究结果表明，类似的结构作用可能是由于其他ZP结构域蛋白在不同分支器官的形成。
The formation of branched epithelial networks is fundamental to the development of many organs, such as the lung, the kidney or the vasculature. Little is known about the mechanisms that control cell rearrangements during tubulogenesis and regulate the size of individual tubes. Recent studies indicate that whereas the basal surface of tube cells interacts with the surrounding tissues and helps to shape the ramification pattern of tubular organs, the apical surface has an important role in the regulation of tube diameter and tube growth. Here we report that two proteins, Piopio (Pio) and Dumpy (Dp), containing a zona pellucida (ZP) domain are essential for the generation of the interconnected tracheal network in Drosophila melanogaster. Pio is secreted apically, accumulates in the tracheal lumen and possibly interacts with Dp through the ZP domains. In the absence of Pio and Dp, multicellular tubes do not rearrange through cell elongation and cell intercalation to form narrow tubes with autocellular junctions; instead they are transformed into multicellular cysts, which leads to a severe disruption of the branched pattern. We propose that an extracellular matrix containing Pio and Dp provides a structural network in the luminal space, around which cell rearrangements can take place in an ordered fashion without losing interconnections. Our results suggest that a similar structural role might be attributed to other ZP-domain proteins in the formation of different branched organs.