Terminal regions of beta-catenin come into view

Abstract

β-catenin is remarkably multifunctional, acting in adhesion, cytoskeletal regulation, and Wnt signaling. In this issue, Xing et al. (2008) present the full-length structure of β-catenin, providing a clearer picture of how these terminal regions modulate β-catenin activities.

Figure 1. Partners and Structure of β-Catenin

(A) Line diagram of β-catenin arm repeat and terminal regions with key binding partners. (B) Structure of full-length β-catenin revealing HelixC (red); unstructured N- and C-terminal regions shown as dotted lines. See Xing et al. (2008) for details.