Crossveinless 2 contains cysteine-rich domains and is required for high levels of BMP-like activity during the formation of the cross veins in Drosophila.

Crossveinless 2 contains cysteine-rich domains and is required for high levels of BMP-like activity during the formation of the cross veins in Drosophila.
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DOI:
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发表时间:
2000-09
期刊:
影响因子:
4.6
通讯作者:
C. Conley;Ross Silburn;Matthew A. Singer;Amy Ralston;Dan Rohwer-Nutter;David J. Olson;William Gelbart;S. Blair
C. Conley;Ross Silburn;Matthew A. Singer;Amy Ralston;Dan Rohwer-Nutter;David J. Olson;William Gelbart;S. Blair
中科院分区:
生物学2区
文献类型:
--
作者:
C. Conley;Ross Silburn;Matthew A. Singer;Amy Ralston;Dan Rohwer-Nutter;David J. Olson;William Gelbart;S. Blair

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由配体Dpp和Gbb介导的BMP样信号传导需要加强果蝇翅膀中大多数静脉的发育。然而,横静脉的形成对BMP样信号的减少特别敏感。我们在这里表明,最终的横脉的形成后发生的纵向静脉在一个过程中,需要本地化的BMP样活动的初始规格。由于Dpp和Gbb水平在横脉发育的早期阶段不可检测地更高,其他因素显然解释了这种局部活性。我们的证据表明,crossveinless 2基因的产物是BMP样信号传导途径的新成员,其需要增强横脉中Dpp信号传导的Gbb。crossveinless 2在发育中的横脉中以较高水平表达,并且是局部BMP样活性所必需的。Crossveinless 2蛋白含有一个假定的信号或跨膜序列,和一个部分的血管性血友病因子D结构域类似于那些已知的调节分子内和分子间键的形成。它还含有五个富含半胱氨酸的结构域,类似于已知结合BMP样配体的Chordin、Short Gastrulation和Procollagen中发现的富含半胱氨酸的结构域。这些特征强烈地表明,Crossveinless 2在细胞外或分泌途径中起作用以直接增强Dpp或Gbb信号传导。
The BMP-like signaling mediated by the ligands Dpp and Gbb is required to reinforce the development of most veins in the Drosophila wing. However, the formation of the cross veins is especially sensitive to reductions in BMP-like signaling. We show here that the formation of the definitive cross veins occurs after the initial specification of the longitudinal veins in a process that requires localized BMP-like activity. Since Dpp and Gbb levels are not detectably higher in the early phases of cross vein development, other factors apparently account for this localized activity. Our evidence suggests that the product of the crossveinless 2 gene is a novel member of the BMP-like signaling pathway required to potentiate Gbb of Dpp signaling in the cross veins. crossveinless 2 is expressed at higher levels in the developing cross veins and is necessary for local BMP-like activity. The Crossveinless 2 protein contains a putative signal or transmembrane sequence, and a partial Von Willebrand Factor D domain similar to those known to regulate the formation of intramolecular and intermolecular bonds. It also contains five cysteine-rich domains, similar to the cysteine-rich domains found in Chordin, Short Gastrulation and Procollagen that are known to bind BMP-like ligands. These features strongly suggest that Crossveinless 2 acts extracelluarly or in the secretory pathway to directly potentiate Dpp or Gbb signaling.