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- W1487123743 abstract "The DEP domain of Dishevelled (Dvl) proteins transduces signals to effector proteins downstream of Dvl in the Wnt pathway. Here we report that DEP-containing mutants inhibit Wnt-induced, but not Dvl-induced, activation of the transcription factor Lef-1. This inhibitory effect is weakened by a K434M mutation. Nuclear magnetic resonance spectroscopy revealed that the DEP domain of mouse Dvl1 comprises a three-helix bundle, a β-hairpin `arm' and two short β-strands at the C-terminal region. Lys 434 is located at the tip of the β-hairpin `arm'. Based on our findings, we conclude that DEP interacts with regulators upstream of Dvl via a strong electric dipole on the molecule's surface created by Lys 434, Asp 445 and Asp 448; the electric dipole and the putative membrane binding site are at two different locations." @default.
- W1487123743 created "2016-06-24" @default.
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- W1487123743 date "2000-12-01" @default.
- W1487123743 modified "2023-10-16" @default.
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- W1487123743 doi "https://doi.org/10.1038/82047" @default.
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