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

被引：173

作者：

Kikuchi, A ^{[1
]}

Kishida, S ^{[1
]}

Yamamoto, H ^{[1
]}

机构：

[1] Hiroshima Univ, Grad Sch Biomed Sci, Dept Biochem, Minami Ku, Hiroshima 7348551, Japan

来源：

EXPERIMENTAL AND MOLECULAR MEDICINE | 2006年 / 38卷 / 01期

关键词：

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

D O I：

10.1038/emm.2006.1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1 / 10

页数：10

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