ArticleNature communications2021
Architecture of the Sema3A/PlexinA4/Neuropilin tripartite complex.
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 27 papers.
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Who cites it
27 citing papers in PubMed, 51 citations in OpenAlex.
- Mechanisms of VEGFR2 activation by VEGF, neuropilin, and heparin.Science advances · 2026Article
- Impact of Sema3A Interference on Cerebellum-Dependent Motor Associative Learning and Memory.International journal of molecular sciences · 2026Article
- CytoSignal detects locations and dynamics of ligand-receptor signaling at cellular resolution from spatial transcriptomic data.Nature genetics · 2026Article
- Neuronal guidance signaling in neurodegenerative diseases: Key regulators that function at neuron-glia and neuroimmune interfaces.Neural regeneration research · 2026Article
- Silencing MALAT1 represses pathological progression, inflammation, and vascular smooth muscle cell phenotype switching by regulating the SEMA3C-mediated Smad pathway in intracranial aneurysms.Frontiers in cellular neuroscience · 2026Article
- [Construction of a highly efficient HBV infection cell model based on HBV co-receptor neuropilin-1].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2025Article
- High-throughput discovery of transmembrane helix dimers from human single-pass membrane proteins with TOXGREEN sort-seq.PNAS nexus · 2025Article
- A unifying mechanism for presynaptic homeostatic plasticity at mammalian peripheral and central synapses.Neuron · 2025Article
- Expanding ligand-receptor interaction networks for axon guidance: Structural insights into signal crosstalk and specificity.Current opinion in neurobiology · 2025Review
- Semaphorin 3A on Osteoporosis: An Overreview of the Literature.Calcified tissue international · 2025Review
- Semaphorin heterodimerization in cis regulates membrane targeting and neocortical wiring.Nature communications · 2024Article
- Molecular mechanisms of proteoglycan-mediated semaphorin signaling in axon guidance.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- NRP1 is a receptor for mammalian orthoreovirus engaged by distinct capsid subunits.Cell host & microbe · 2024Article
- Structure and function of Semaphorin-5A glycosaminoglycan interactions.Nature communications · 2024Article
- Hallmarks of perineural invasion in pancreatic ductal adenocarcinoma: new biological dimensions.Frontiers in oncology · 2024Review
- Role of Semaphorin 3A in Kidney Development and Diseases.Diagnostics (Basel, Switzerland) · 2023Review
- A single-cell atlas of West African lungfish respiratory system reveals evolutionary adaptations to terrestrialization.Nature communications · 2023Article
- New Crystal Form of Human Neuropilin-1 b1 Fragment with Six Electrostatic Mutations Complexed with KDKPPR Peptide Ligand.Molecules (Basel, Switzerland) · 2023Article
- Semaphorin3A Exacerbates Cardiac Microvascular Rarefaction in Pressure Overload-Induced Heart Disease.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Neuropilin 1 (NRP1) Positively Regulates Adipogenic Differentiation in C3H10T1/2 Cells.International journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Secreted class 3 semaphorins (Sema3s) form tripartite complexes with the plexin receptor and neuropilin coreceptor, which are both transmembrane proteins that together mediate semaphorin signal for neuronal axon guidance and other processes. Despite extensive investigations, the overall architecture of and the molecular interactions in the Sema3/plexin/neuropilin complex are incompletely understood. Here we present the cryo-EM structure of a near intact extracellular region complex of Sema3A, PlexinA4 and Neuropilin 1 (Nrp1) at 3.7 Å resolution. The structure shows a large symmetric 2:2:2 assembly in which each subunit makes multiple interactions with others. The two PlexinA4 molecules in the complex do not interact directly, but their membrane proximal regions are close to each other and poised to promote the formation of the intracellular active dimer for signaling. The structure reveals a previously unknown interface between the a2b1b2 module in Nrp1 and the Sema domain of Sema3A. This interaction places the a2b1b2 module at the top of the complex, far away from the plasma membrane where the transmembrane regions of Nrp1 and PlexinA4 embed. As a result, the region following the a2b1b2 module in Nrp1 must span a large distance to allow the connection to the transmembrane region, suggesting an essential role for the long non-conserved linkers and the MAM domain in neuropilin in the semaphorin/plexin/neuropilin complex.
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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.