ArticleProceedings of the National Academy of Sciences of the United States of America2019
Structural characterization of an activin class ternary receptor complex reveals a third paradigm for receptor specificity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 37 citations in OpenAlex.
- The crystal structure of the activin B:Fst288 complex and computational insights into the broad antagonistic activity and specificity of follistatin.The Journal of biological chemistry · 2026Article
- Inhibition of TGF-β signaling in microglia stimulates hippocampal adult neurogenesis and reduces anxiety-like behavior in adult mice.Nature communications · 2026Article
- The crystal structure of the activin B:Fst288 complex and computational insights into the broad antagonistic activity and specificity of follistatin.bioRxiv : the preprint server for biology · 2025Article
- 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
- Molecular mechanism of Activin receptor inhibition by DLK1.Nature communications · 2025Article
- Dual signaling pathways of TGF-β superfamily cytokines in hepatocytes: balancing liver homeostasis and disease progression.Frontiers in pharmacology · 2025Review
- Stepwise release of Activin-A from its inhibitory prodomain is modulated by cysteines and requires furin coexpression to promote melanoma growth.Communications biology · 2024Article
- Article
- Activin E is a transforming growth factor β ligand that signals specifically through activin receptor-like kinase 7.The Biochemical journal · 2024Article
- Review
- Article
- How Activin A Became a Therapeutic Target in Fibrodysplasia Ossificans Progressiva.Biomolecules · 2024Review
- Synthesis ofOrganic & biomolecular chemistry · 2023Article
- Functional comparison of human ACVR1 and zebrafish Acvr1l FOP-associated variants in embryonic zebrafish.Developmental dynamics : an official publication of the American Association of Anatomists · 2023Article
- Blockade of Activin Receptor IIB Protects Arthritis Pathogenesis by Non-Amplification of Activin A-ACVR2B-NOX4 Axis Pathway.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Functional substitutions of amino acids that differ between GDF11 and GDF8 impact skeletal development and skeletal muscle.Life science alliance · 2023Article
- Evolving roles of activins and inhibins in ovarian cancer pathophysiology.American journal of physiology. Cell physiology · 2023Review
- A versatile Halo- and SNAP-tagged BMP/TGFβ receptor library for quantification of cell surface ligand binding.Communications biology · 2023Article
- Follistatin Forms a Stable Complex With Inhibin A That Does Not Interfere With Activin A Antagonism.Endocrinology · 2023Article
- Sex specificity of pancreatic cancer cachexia phenotypes, mechanisms, and treatment in mice and humans: role of Activin.Journal of cachexia, sarcopenia and muscle · 2022Article
Corrections and comments
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Authors and funding
15 authors at 5 institutions in 1 country.
Funding
Abstract
TGFβ family ligands, which include the TGFβs, BMPs, and activins, signal by forming a ternary complex with type I and type II receptors. For TGFβs and BMPs, structures of ternary complexes have revealed differences in receptor assembly. However, structural information for how activins assemble a ternary receptor complex is lacking. We report the structure of an activin class member, GDF11, in complex with the type II receptor ActRIIB and the type I receptor Alk5. The structure reveals that receptor positioning is similar to the BMP class, with no interreceptor contacts; however, the type I receptor interactions are shifted toward the ligand fingertips and away from the dimer interface. Mutational analysis shows that ligand type I specificity is derived from differences in the fingertips of the ligands that interact with an extended loop specific to Alk4 and Alk5. The study also reveals differences for how TGFβ and GDF11 bind to the same type I receptor, Alk5. For GDF11, additional contacts at the fingertip region substitute for the interreceptor interactions that are seen for TGFβ, indicating that Alk5 binding to GDF11 is more dependent on direct contacts. In support, we show that a single residue of Alk5 (Phe
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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.