Secondary structure, ¹H, ¹³C and ¹⁵N resonance assignments and molecular interactions of the dishevelled DIX domain

DGS Capelluto, Michael Overduin

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)243-7
Number of pages5
JournalJournal of biochemistry and molecular biology
Volume38
Issue number2
Publication statusPublished - 31 Mar 2005

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