Regulation of Wnt signaling by protein-protein interaction and post-translational modifications.
- Author:
Akira KIKUCHI
1
;
Shosei KISHIDA
;
Hideki YAMAMOTO
Author Information
1. Department of Biochemistry, Graduate School of Biomedical Sciences, Hiroshima University, 1-2-3 Kasumi, Minami-ku, Hiroshima 734-8551, Japan. akikuchi@hiroshima-u.ac.jp
- Publication Type:Review
- Keywords:
beta catenin;
protein interaction mapping;
protein processing;
post-translational;
TCF transcription factors;
Wnt proteins
- MeSH:
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
- From:Experimental & Molecular Medicine
2006;38(1):1-10
- CountryRepublic of Korea
- Language:English
-
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.
