ArticleNature communications2021
Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 58 citations in OpenAlex.
- Heterotopic Ossification: Molecular Drivers, Subtype-Specific Mechanisms, and Translational Therapeutic Advances.Biomolecules · 2026Review
- Caspase-1 Mediated Cleavage of BMP Type I Receptor Drives BMP2-Induced Differentiation of Bone Marrow Mesenchymal Stem Cells into Adipocytes.Applied sciences (Basel, Switzerland) · 2025Article
- State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025Review
- CryoEM structure of ALK2:BMP6 reveals distinct mechanism that allow ALK2 to interact with both BMP and activin ligands.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Developing HaloTag and SNAP-Tag Chemical Inducers of Dimerization to Probe Receptor Oligomerization and Downstream Signaling.Angewandte Chemie (International ed. in English) · 2025Article
- ALK1-BMPRII agonism by clustering bispecific antibodies treats hereditary hemorrhagic telangiectasia.bioRxiv : the preprint server for biology · 2025Article
- TFAP2A+ embryonic progenitor cells undergo fate diversification to give rise to human amnion, germline, and mesoderm.bioRxiv : the preprint server for biology · 2025Article
- Article
- Adaptation of ACMG/AMP Guidelines for Clinical Classification ofHuman mutation · 2025Article
- Case report: Novel homozygousFrontiers in genetics · 2025Article
- miR-889-3p targeting BMPR2 promotes the development of retinoblastoma via JNK/MAPK/ERK signaling.Scientific reports · 2024Article
- iMSC-mediated delivery of ACVR2B-Fc fusion protein reduces heterotopic ossification in a mouse model of fibrodysplasia ossificans progressiva.Stem cell research & therapy · 2024Article
- Brain-Derived Neurotrophic Factor - The Protective Agent Against Neurological Disorders.CNS & neurological disorders drug targets · 2024Article
- BMP signaling in cancer stemness and differentiation.Cell regeneration (London, England) · 2023Review
- Computational and Experimental Analyses for Pathogenicity Prediction ofJournal of clinical medicine · 2023Article
- Polypeptide Substrate Accessibility Hypothesis: Gain-of-Function R206H Mutation Allosterically Affects Activin Receptor-like Protein Kinase Activity.Biomolecules · 2023Article
- A blocking monoclonal antibody reveals dimerization of intracellular domains of ALK2 associated with genetic disorders.Nature communications · 2023Article
- Contemporary perspectives on heterotopic ossification.JCI insight · 2022Review
- Competition between type I activin and BMP receptors for binding to ACVR2A regulates signaling to distinct Smad pathways.BMC biology · 2022Article
- Anti-Müllerian Hormone Signal Transduction involved in Müllerian Duct Regression.Frontiers in endocrinology · 2022Review
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
Upon ligand binding, bone morphogenetic protein (BMP) receptors form active tetrameric complexes, comprised of two type I and two type II receptors, which then transmit signals to SMAD proteins. The link between receptor tetramerization and the mechanism of kinase activation, however, has not been elucidated. Here, using hydrogen deuterium exchange mass spectrometry (HDX-MS), small angle X-ray scattering (SAXS) and molecular dynamics (MD) simulations, combined with analysis of SMAD signaling, we show that the kinase domain of the type I receptor ALK2 and type II receptor BMPR2 form a heterodimeric complex via their C-terminal lobes. Formation of this dimer is essential for ligand-induced receptor signaling and is targeted by mutations in BMPR2 in patients with pulmonary arterial hypertension (PAH). We further show that the type I/type II kinase domain heterodimer serves as the scaffold for assembly of the active tetrameric receptor complexes to enable phosphorylation of the GS domain and activation of SMADs.
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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.