Secondary structure, 1H, 13C and 15N resonance assignments and molecular interactions of the dishevelled DIX domain.
Dishevelled (Dvl) is a positive regulator of the canonical Wnt signaling pathway, which regulates the levels of beta-catenin. The beta-catenin oncoprotein depends upon the association of Dvl and Axin proteins through their DIX domains, and its accumulation directs the expression of specific developmental-related genes at the nucleus. Here, the (1)H, (13)C and (15)N resonances of the human Dishevelled 2 DIX domain are assigned using heteronuclear nuclear magnetic resonance (NMR) spectroscopy. In addition, helical and extended elements are identified based on the NMR data. The results establish a structural context for characterizing the actin and phospholipid interactions and binding sites of this novel domain, and provide insights into its role in protein localization to stress fibers and cytoplasmic vesicles during Wnt signaling.
Capelluto
Daniel G S
DG
Department of Pharmacology, University of Colorado Health Science Center at Fitzsimmons, Aurora, CO 80045, USA.
Overduin
Michael
M
D048868:Adaptor Proteins, Signal Transducing; D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D017124:Conserved Sequence; D000072261:Dishevelled Proteins; D006801:Humans; D006859:Hydrogen; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D010750:Phosphoproteins; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment
D048868:Adaptor Proteins, Signal Transducing; D002247:Carbon Isotopes; C000606581:DVL2 protein, human; D000072261:Dishevelled Proteins; D009587:Nitrogen Isotopes; D010750:Phosphoproteins; D011506:Proteins; D006859:Hydrogen