Homomeric and heteromeric complexes among TGF-β and BMP receptors and their roles in signaling

被引：73

作者：

Ehrlich, Marcelo ^{[2
]}

Horbelt, Daniel ^{[3
]}

Marom, Barak ^{[1
]}

Knaus, Petra ^{[3
]}

Henis, Yoav I. ^{[1
]}

机构：

[1] Tel Aviv Univ, George S Wise Fac Life Sci, Dept Neurobiol, IL-69978 Tel Aviv, Israel

[2] Tel Aviv Univ, George S Wise Fac Life Sci, Dept Cell Res & Immunol, IL-69978 Tel Aviv, Israel

[3] Free Univ Berlin, Inst Chem & Biochem, D-1495 Berlin, Germany

来源：

CELLULAR SIGNALLING | 2011年 / 23卷 / 09期

基金：

以色列科学基金会;

关键词：

TGF-beta; BMP; Receptor oligomerization; Patch-FRAP; Protein-protein interactions; Signaling; GROWTH-FACTOR-BETA; BONE MORPHOGENETIC PROTEIN; CRYSTAL-STRUCTURE; II RECEPTOR; EXTRACELLULAR DOMAIN; ACTIVIN RECEPTOR; OSTEOGENIC PROTEIN-1; SMAD1/5; PHOSPHORYLATION; 3-DIMENSIONAL STRUCTURE; OLIGOMERIC STRUCTURE;

D O I：

10.1016/j.cellsig.2011.04.004

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Transforming growth factor-beta (TGF-beta) ligands and bone morphogenetic proteins (BMPs) play myriad roles in many biological processes and diseases. Their pluripotent activities are subject to multiple levels of regulation, including receptor oligomerization, endocytosis, association with co-receptors, cellular scaffolds or membrane domains, as well as transcriptional control. In this review, we focus on TGF-beta and BMP receptor homomeric and heterorneric complex formation and their modulation by ligand binding, which regulate signaling on a near-immediate timescale. We discuss the current structural, biochemical and biophysical evidence for the oligomerization of these receptors, and the potential roles of distinct oligomeric interactions in signaling. (C) 2011 Elsevier Inc. All rights reserved.

引用

页码：1424 / 1432

页数：9

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