Wnt Stabilization of β-Catenin Reveals Principles for Morphogen Receptor-Scaffold Assemblies

Author:

Kim Sung-Eun1,Huang He1,Zhao Ming2,Zhang Xinjun1,Zhang Aili23,Semonov Mikhail V.1,MacDonald Bryan T.1,Zhang Xiaowu4,Abreu Jose Garcia15,Peng Leilei2,He Xi1

Affiliation:

1. F. M. Kirby Center, Boston Children’s Hospital, Harvard Medical School, Boston, MA 02115, USA.

2. College of Optical Sciences, University of Arizona, Tucson, AZ 85721, USA.

3. School of Biomedical Engineering, Jiaotong University, Shanghai, China.

4. Cell Signaling Technology, Danvers, MA 01923, USA.

5. Instituto de Ciencias Biomedicas, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.

Abstract

Signal Scaffolds Scaffolds in cellular signaling pathways are turning out to do way more than just hold proteins together in a complex. Kim et al. (p. 867 , published online 11 April) showed the importance of the scaffold protein Axin as an active participant controlling the kinetics of activation of signaling through the pathways. Axin is part of two protein complexes that have opposing actions that may regulate the timing of signaling—either activating Wnt signaling, thus protecting β-catenin from destruction, or causing proteolytic destruction of β-catenin. Rock et al. (p. 871 , published online 11 April) characterized the role of the scaffold protein Nud1 in the mitotic exit network and found that the kinase that produces the output from the signaling complex only interacts with a scaffold that is primed by its activator protein kinase, already bound to the scaffold and creating a docking site.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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