Unwinding a path to nuclear beta-catenin.
In this issue of Cell, Yang et al. (2006b) show that PDGF, a growth factor that induces the transition of epithelial cells to mesenchymal cells, stimulates the c-Abl kinase-dependent phosphorylation of p68 RNA helicase. Phosphorylated p68 dissociates beta-catenin from the Axin destruction complex, thereby promoting nuclear beta-catenin signaling independent of Wnt activation.
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Xi
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Program of Neurobiology, Children's Hospital Boston, Harvard Medical School, 300 Longwood Avenue, Boston, MA 02115 USA. xi.he@childrens.harvard.edu
D000818:Animals; D060466:Axin Protein; D002454:Cell Differentiation / Q000502:physiology; D002467:Cell Nucleus / Q000737:chemistry / Q000378:metabolism; D053487:DEAD-box RNA Helicases / Q000378:metabolism*; D006801:Humans; D010982:Platelet-Derived Growth Factor / Q000378:metabolism; D016315:Proto-Oncogene Proteins c-abl / Q000378:metabolism; D012097:Repressor Proteins / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology*; D051153:Wnt Proteins / Q000378:metabolism; D051176:beta Catenin / Q000378:metabolism*
D060466:Axin Protein; D010982:Platelet-Derived Growth Factor; D012097:Repressor Proteins; D051153:Wnt Proteins; D051176:beta Catenin; D016315:Proto-Oncogene Proteins c-abl; D053487:DEAD-box RNA Helicases