Exp Mol Med.  2006 Feb;38(1):1-10.

Regulation of Wnt signaling by protein-protein interaction and post-translational modifications

Affiliations
  • 1Department of Biochemistry, Graduate School of Biomedical Sciences, Hiroshima University, 1-2-3 Kasumi, Minami-ku, Hiroshima 734-8551, Japan. akikuchi@hiroshima-u.ac.jp

Abstract

The Wnt signaling pathway is conserved in various species from worms to mammals, and plays important roles in cellular proliferation, differentiation, and migration. Wnt stabilizes cytoplasmic beta-catenin and then the accumulated beta-catenin is translocated into the nucleus, where it activates the transcriptional factor T-cell factor (Tcf)/lymphoid enhancer factor (Lef), and thereby stimulates the expression of genes including c-myc, c-jun, fra-1, and cyclin D1. Tight regulation of this response involves post-translational modifications of the components of the Wnt signaling pathway. Phosphorylation, ubiquitination, and sumoylation have been shown to affect the half-life of beta-catenin and the transcriptional activity of Tcf/Lef. The precise spatio-temporal patterns of these multiple modifications determine the driving force of various cellular responses.

Keyword

beta catenin; protein interaction mapping; protein processing; post-translational; TCF transcription factors; Wnt proteins

MeSH Terms

Animals
Binding Sites
Gene Expression Regulation
Humans
Models, Biological
Protein Binding
*Protein Processing, Post-Translational
*Signal Transduction
TCF Transcription Factors
*Trans-Activators
Wnt Proteins/classification/genetics/*metabolism
beta Catenin
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