Multiplicity of the interactions of Wnt proteins and their receptors

被引：239

作者：

Kikuchi, Akira ^{[1
]}

Yamamoto, Hideki ^{[1
]}

Kishida, Shosei ^{[1
]}

机构：

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

来源：

CELLULAR SIGNALLING | 2007年 / 19卷 / 04期

关键词：

Wnt; low-density-lipoprotein receptor-related protein 5/6; frizzled; post-translational modification; endocytosis;

D O I：

10.1016/j.cellsig.2006.11.001

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 [细胞生物学]; 090102 [作物遗传育种];

摘要：

Wnts are secreted proteins that are essential for a wide array of developmental and physiological processes. They signal across the plasma membranes by interacting with serpentine receptors of the Frizzled (Fz) family and members of the low-density-lipoprotein receptor-related protein (LRP) family. Recent advances in the Wnt signaling field have revealed that Wnt-unrelated proteins activate or suppress Wnt signaling by binding to Fzs or LRP5/6 and that atypical receptor tyrosine kinases mediate Wnt signaling independently of Fz and/or function as a Fz co-receptor. This review highlights recent progress in our understanding of the multiplicity of Wnts and their receptors. We discuss how the interaction between the ligands and receptors activate distinct intracellular signaling pathways. We also discuss how intracellular trafficking of Wnt signaling components can regulate the sensitivity of cells to Wnts. (c) 2006 Elsevier Inc. All rights reserved.

引用

页码：659 / 671

页数：13

共 128 条

[1]

Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process [J].