Wnt-dependent assembly of supermolecular Dishevelled-3-based complexes
作者： N. Yokoyama , U. Golebiewska , H.-y. Wang , C. C. Malbon
DOI: 10.1242/JCS.075275
关键词: Signal transducing adaptor protein 、 Scaffold protein 、 Cell biology 、 Biology 、 Wnt signaling pathway 、 Plasma protein binding 、 Proteomics 、 Molecular mass 、 Fluorescence microscope 、 Dishevelled
摘要: Dishevelled-3 (Dvl3) is a multivalent scaffold protein that essential to Wnt signaling during development. Although Dvl-based punctae have been visualized by fluorescence microscopy; the physical nature and dynamic character of such complexes are enigmatic. We use steric-exclusion chromatography, affinity pull-downs, proteomics correlation microscopy characterize supermolecular Dvl3-based totipotent mouse F9 cells. The molecular mass ranges from homodimeric Dvl3 well-defined peaks harboring 0.4 2.0 MDa. Addition Wnt3a stimulates formation greater within 30 minutes. presence DKK1 knockdown Dishevelled proteins block 2 MDa also stimulation canonical pathway. Fluorescent identified with >30 in live cells; these were provoked form structures even Wnt3a. establish for first time functional very large, complexes.
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