ArticleThe Journal of biological chemistry2011
Formation of stable homomeric and transient heteromeric bone morphogenetic protein (BMP) receptor complexes regulates Smad protein signaling.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 38 citations in OpenAlex.
- Heterotopic Ossification: Molecular Drivers, Subtype-Specific Mechanisms, and Translational Therapeutic Advances.Biomolecules · 2026Review
- Dual signaling pathways of TGF-β superfamily cytokines in hepatocytes: balancing liver homeostasis and disease progression.Frontiers in pharmacology · 2025Review
- Article
- NRP1 interacts with endoglin and VEGFR2 to modulate VEGF signaling and endothelial cell sprouting.Communications biology · 2024Article
- Cholesterol modulates type I/II TGF-β receptor complexes and alters the balance between Smad and Akt signaling in hepatocytes.Communications biology · 2024Article
- Polypeptide Substrate Accessibility Hypothesis: Gain-of-Function R206H Mutation Allosterically Affects Activin Receptor-like Protein Kinase Activity.Biomolecules · 2023Article
- A versatile Halo- and SNAP-tagged BMP/TGFβ receptor library for quantification of cell surface ligand binding.Communications biology · 2023Article
- Competition between type I activin and BMP receptors for binding to ACVR2A regulates signaling to distinct Smad pathways.BMC biology · 2022Article
- Local BMP signaling: A sensor for synaptic activity that balances synapse growth and function.Current topics in developmental biology · 2022Review
- ALK1 regulates the internalization of endoglin and the type III TGF-β receptor.Molecular biology of the cell · 2021Article
- Article
- Chemotropic signaling by BMP7 requires selective interaction at a key residue in ActRIIA.Biology open · 2019Article
- Heparan sulfate antagonism alters bone morphogenetic protein signaling and receptor dynamics, suggesting a mechanism in hereditary multiple exostoses.The Journal of biological chemistry · 2018Article
- Stiffness-dependent cellular internalization of matrix-bound BMP-2 and its relation to Smad and non-Smad signaling.Acta biomaterialia · 2016Article
- Tuning cellular responses to BMP-2 with material surfaces.Cytokine & growth factor reviews · 2016Review
- A Novel, Noncanonical BMP Pathway Modulates Synapse Maturation at the Drosophila Neuromuscular Junction.PLoS genetics · 2016Article
- TβRIII independently binds type I and type II TGF-β receptors to inhibit TGF-β signaling.Molecular biology of the cell · 2015Article
- Regulation of TGF-β receptor hetero-oligomerization and signaling by endoglin.Molecular biology of the cell · 2015Article
- Antibody-directed coupling of endoglin and MMP-14 is a key mechanism for endoglin shedding and deregulation of TGF-β signaling.Oncogene · 2014Article
- SMAD versus non-SMAD signaling is determined by lateral mobility of bone morphogenetic protein (BMP) receptors.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The type I and type II bone morphogenetic protein receptors (BMPRI and BMPRII) are present at the plasma membrane as monomers and homomeric and heteromeric complexes, which are modulated by ligand binding. The complexes of their extracellular domains with ligand were shown to form heterotetramers. However, the dynamics of the oligomeric interactions among the full-length receptors in live cell membranes were not explored, and the roles of BMP receptor homodimerization were unknown. Here, we investigated these issues by combining patching/immobilization of an epitope-tagged BMP receptor at the cell surface with measurements of the lateral diffusion of a co-expressed, differently tagged BMP receptor by fluorescence recovery after photobleaching (FRAP). These studies led to several novel conclusions. (a) All homomeric complexes (without or with BMP-2) were stable on the patch/FRAP time scale (minutes), whereas the heterocomplexes were transient, a difference that may affect signaling. (b) Patch/FRAP between HA- and myc-tagged BMPRII combined with competition by untagged BMPRIb showed that the heterocomplexes form at the expense of homodimers. (c) Stabilization of BMPRII·BMPRIb heterocomplexes (but not homomeric complexes) by IgG binding to same-tag receptors elevated phospho-Smad formation both without and with BMP-2. These findings suggest two mechanisms that may suppress the tendency of preformed BMP receptor hetero-oligomers to signal without ligand: (a) competition between homo- and heterocomplex formation, which reduces the steady-state level of the latter, and (b) the transient nature of the heterocomplexes, which limits the time during which BMPRI can be phosphorylated by BMPRII in the heterocomplex.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.