Regulation of Wnt signaling by protein-protein interaction and post-translational modifications
Experimental & Molecular Medicine
;
: 1-10, 2006.
Article
in English
| WPRIM
| ID: wpr-77907
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Protein Binding
/
Binding Sites
/
Signal Transduction
/
Trans-Activators
/
Protein Processing, Post-Translational
/
Gene Expression Regulation
/
Wnt Proteins
/
Beta Catenin
/
TCF Transcription Factors
/
Models, Biological
Type of study:
Prognostic study
Limits:
Animals
/
Humans
Language:
English
Journal:
Experimental & Molecular Medicine
Year:
2006
Type:
Article
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