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Figure 4


Fig. 4. The recruitment of axin into Dvl2 puncta depends on the DIX but not the DAX domain. (A-E) COS-7 cells co-expressing wt and mutant axin (left-hand panels, and red) and Dvl2 (middle panels, and green) as indicated (merges in right-hand panels), fixed and stained with antibodies against Dvl2 and (A,E) HA. Axin colocalises precisely with Dvl2 puncta (A), regardless of its DAX domain (B), but dependent on a functional DIX domain of Dvl2 (C,D; the {Delta}DIX construct used here also contains the TPR dimerisation domain, but this domain does not detectably change its behaviour or subcellular distribution; not shown). Note that two sets of puncta are observed if the DIX domain is co-expressed with axin, indicating that the DIX and DAX domains do not interact directly. (F) Pull-down assays between bacterially expressed GST-tagged DIX domain and in vitro translated HA-tagged axin or Dvl2, as indicated (GST input proteins are shown on the right). The DIX domain binds efficiently to itself (within full-length HA-Dvl2, arrow), but not to the DAX domain (within full-length HA-axin, arrow). Scale bar, 15 µm.





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