Grosshans J, Schnorrer F, Nüsslein-Volhard C
Max-Planck-Institut für Entwicklungsbiologie, Abteilung III (Genetik), Spemannstrasse 35/III, D-72076, Tübingen, Germany.
Mech Dev. 1999 Mar;81(1-2):127-38. doi: 10.1016/s0925-4773(98)00236-6.
In the Drosophila embryo the nuclear localisation of Dorsal, a member of the Rel family, is regulated by an extracellular signal, which is transmitted to the interior of the egg cell by a cascade of proteins involving the novel protein Tube and the protein kinase Pelle. Here we analyse the activation mechanism of Tube and Pelle and the interaction between these two components. We show that both proteins, although having different biochemical activities, are activated by the same mechanism. Membrane association alone is not sufficient, but oligomerisation is required for full activation of Tube and Pelle. By deletion analysis we determined the domains of Tube and Pelle mediating the physical interaction and the signalling to downstream components. In order to investigate the link between Pelle and the target of the signalling cascade, the Dorsal/Cactus complex, we isolated and characterised the novel, but evolutionary conserved protein Pellino, which associates with the kinase domain of Pelle.
在果蝇胚胎中,Rel家族成员背腹蛋白(Dorsal)的核定位受一种细胞外信号调控,该信号通过一系列蛋白质传递到卵细胞内部,这一系列蛋白质包括新蛋白Tube和蛋白激酶Pelle。在此,我们分析了Tube和Pelle的激活机制以及这两种成分之间的相互作用。我们发现,这两种蛋白质虽然具有不同的生化活性,但通过相同的机制被激活。仅膜结合并不足够,Tube和Pelle的完全激活需要寡聚化。通过缺失分析,我们确定了Tube和Pelle介导物理相互作用以及向下游成分信号传导的结构域。为了研究Pelle与信号级联反应的靶标背腹蛋白/仙人掌蛋白复合物(Dorsal/Cactus complex)之间的联系,我们分离并鉴定了新的但在进化上保守的蛋白质Pellino,它与Pelle的激酶结构域相关联。