ArticleThe Journal of biological chemistry2009
Structure and function of the intracellular region of the plexin-b1 transmembrane receptor.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 95 citations in OpenAlex.
- Semaphorins and Their Role in Neuropathic Pain.Life (Basel, Switzerland) · 2026Review
- Recent breakthroughs in understanding the allosteric features of Ras GTPases and their effector and regulatory protein interactions, enabling drug design.Current opinion in structural biology · 2026Review
- Computational model predicts function of Rho-GTPase binding for plexin receptor GAP activity on Rap1b via dynamic allosteric changes.Protein science : a publication of the Protein Society · 2025Article
- Plexin/Semaphorin antagonism orchestrates collective cell migration and organ sculpting by regulating epithelial-mesenchymal balance.Science advances · 2025Article
- Structural Dynamics of Rho GTPases.Journal of molecular biology · 2025Review
- Former smoking associated with epigenetic modifications in human granulosa cells among women undergoing assisted reproduction.Scientific reports · 2024Article
- New Promising Routes in Peptic Ulcers: Toll-like Receptors and Semaphorins.Endocrine, metabolic & immune disorders drug targets · 2024Review
- Plexin-mediated neuronal development and neuroinflammatory responses in the nervous system.Histology and histopathology · 2023Review
- Clearance phagocytosis by the retinal pigment epithelial during photoreceptor outer segment renewal: Molecular mechanisms and relation to retinal inflammation.Immunological reviews · 2023Review
- Plexin-B1 Mutation Drives Metastasis in Prostate Cancer Mouse Models.Cancer research communications · 2023Article
- Cryo-electron Microscopic Analysis of Single-Pass Transmembrane Receptors.Chemical reviews · 2022Review
- PLXNB1 mutations in the etiology of idiopathic hypogonadotropic hypogonadism.Journal of neuroendocrinology · 2022Article
- Architecture of the Sema3A/PlexinA4/Neuropilin tripartite complex.Nature communications · 2021Article
- Mutant Presenilin 1 Dysregulates Exosomal Proteome Cargo Produced by Human-Induced Pluripotent Stem Cell Neurons.ACS omega · 2021Article
- Evolution and Diversity of Semaphorins and Plexins in Choanoflagellates.Genome biology and evolution · 2021Article
- Plexin-Bs enhance their GAP activity with a novel activation switch loop generating a cooperative enzyme.Cellular and molecular life sciences : CMLS · 2021Article
- Structural basis of semaphorin-plexin cis interaction.The EMBO journal · 2020Article
- Article
- Making Connections: Guidance Cues and Receptors at Nonneural Cell-Cell Junctions.Cold Spring Harbor perspectives in biology · 2018Review
- Semaphorin4D-PlexinB1 Signaling Attenuates Photoreceptor Outer Segment Phagocytosis by Reducing Rac1 Activity of RPE Cells.Molecular neurobiology · 2018Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 3 countries.
Funding
Abstract
Members of the plexin family are unique transmembrane receptors in that they interact directly with Rho family small GTPases; moreover, they contain a GTPase-activating protein (GAP) domain for R-Ras, which is crucial for plexin-mediated regulation of cell motility. However, the functional role and structural basis of the interactions between the different intracellular domains of plexins remained unclear. Here we present the 2.4 A crystal structure of the complete intracellular region of human plexin-B1. The structure is monomeric and reveals that the GAP domain is folded into one structure from two segments, separated by the Rho GTPase binding domain (RBD). The RBD is not dimerized, as observed previously. Instead, binding of a conserved loop region appears to compete with dimerization and anchors the RBD to the GAP domain. Cell-based assays on mutant proteins confirm the functional importance of this coupling loop. Molecular modeling based on structural homology to p120(GAP).H-Ras suggests that Ras GTPases can bind to the plexin GAP region. Experimentally, we show that the monomeric intracellular plexin-B1 binds R-Ras but not H-Ras. These findings suggest that the monomeric form of the intracellular region is primed for GAP activity and extend a model for plexin activation.
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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.