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

• Published in: Cellular signalling Vol. 23; no. 9; pp. 1424 - 1432
• Main Authors: Ehrlich, Marcelo, Horbelt, Daniel, Marom, Barak, Knaus, Petra, Henis, Yoav I.
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 01.09.2011
• Subjects: Binding; Biochemistry; BMP; Bone Morphogenetic Protein Receptors - chemistry; bone morphogenetic proteins; Bone Morphogenetic Proteins - metabolism; Bones; Cellular; Control; endocytosis; Fluorescence Recovery After Photobleaching - methods; Gene Expression Regulation; Humans; Ligands; Modulation; Patch-FRAP; Phosphorylation; Protein Binding; Protein Multimerization; Protein–protein interactions; Receptor oligomerization; Receptors; Receptors, Transforming Growth Factor beta - chemistry; Signal Transduction; Signaling; TGF-β; transcription (genetics); Transcriptional Activation; transforming growth factor beta; Transforming Growth Factor beta - metabolism; Signaling; TGF-β; Protein–protein interactions; BMP; Receptor oligomerization; Patch-FRAP
• ISSN: 0898-6568; 1873-3913; 1873-3913
• DOI: 10.1016/j.cellsig.2011.04.004

Transforming growth factor-β (TGF-β) 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-β and BMP receptor homomeric and heteromeric 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.