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Autoinhibition of Dishevelled protein regulated by its extreme C terminus plays a distinct role in Wnt/-catenin and Wnt/planar cell polarity (PCP) signaling pathways

文献类型： 外文期刊

作者： Qi, Jing 1 ; Lee, Ho-Jin 2 ; Saquet, Audrey 6 ; Cheng, Xiao-Ning 1 ; Shao, Ming 1 ; Zheng, Jie J. 2 ; Shi, De-Li 1 ;

作者机构： 1.Shandong Univ, Sch Life Sci, 27 Shanda Nan Rd, Jinan 250100, Peoples R China

2.St Jude Childrens Res Hosp, Dept Biol Struct, 332 N Lauderdale St, Memphis, TN 38105 USA

3.Univ Calif Los Angeles, Dept Ophthalmol, Stein Eye Inst, David Geffen Sch Med, 100 Stein Plaza, Los Angeles, CA 90095 USA

4.Univ Calif Los Angeles, Inst Mol Biol, 100 Stein Plaza, Los Angeles, CA 90095 USA

5.Shandong Acad Agr Sci, Inst Anim Sci & Vet Med, Shandong Key Lab Anim Dis Control & Breeding, Jinan 250100, Peoples R China

6.Univ Paris 06, Sorbonne Univ,UPMC, CNRS,UMR7622, IBPS,Dev Biol Lab, F-75005 Paris, France

关键词： PDZ domain;signal transduction;structural biology;Wnt pathway;Wnt signaling

期刊名称：JOURNAL OF BIOLOGICAL CHEMISTRY （ 影响因子：5.157； 五年影响因子：5.041 ）

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收录情况： SCI

摘要： Dishevelled (Dvl) is a key intracellular signaling molecule that mediates the activation of divergent Wnt pathways. It contains three highly conserved domains known as DIX, PDZ, and DEP, the functions of which have been well characterized in -catenin-dependent canonical and -catenin-independent noncanonical Wnt signaling. The C-terminal region is also highly conserved from invertebrates to vertebrates. However, its function in regulating the activation of different Wnt signals remains unclear. We reported previously that Dvl conformational change triggered by the highly conserved PDZ-binding C terminus is important for the pathway specificity. Here we provide further evidence demonstrating that binding of the C terminus to the PDZ domain results in Dvl autoinhibition in the Wnt signaling pathways. Therefore, the forced binding of the C terminus to the PDZ domain reduces the activity of Dvl in noncanonical Wnt signaling, whereas obstruction of this interaction releases Dvl autoinhibition, impairs its functional interaction with LRP6 in canonical Wnt signaling, and increases its specificity in noncanonical Wnt signaling, which is closely correlated with an enhanced Dvl membrane localization. Our findings highlight the importance of the C terminus in keeping Dvl in an appropriate autoinhibited state, accessible for regulation by other partners to switch pathway specificity. Particularly, the C-terminally tagged Dvl fusion proteins that have been widely used to study the function and cellular localization of Dvl may not truly represent the wild-type Dvl because those proteins cannot be autoinhibited.

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