| Literature DB >> 11101902 |
H C Wong1, J Mao, J T Nguyen, S Srinivas, W Zhang, B Liu, L Li, D Wu, J Zheng.
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 beta-hairpin 'arm' and two short beta-strands at the C-terminal region. Lys 434 is located at the tip of the beta-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.Entities:
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Year: 2000 PMID： 11101902 PMCID： PMC4381838 DOI： 10.1038/82047
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368