RTN4/NoGo-receptor binding to BAI adhesion-GPCRs regulates neuronal development
RTN4-binding proteins were widely studied as “NoGo” receptors, but their physiological interactors and roles remain elusive. Similarly, BAI adhesion-GPCRs were associated with numerous activities, but their ligands and functions remain unclear. Using unbiased approaches, we observed an unexpected co...
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| Published in | Cell Vol. 184; no. 24; pp. 5869 - 5885.e25 |
|---|---|
| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
24.11.2021
Elsevier |
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| Abstract | RTN4-binding proteins were widely studied as “NoGo” receptors, but their physiological interactors and roles remain elusive. Similarly, BAI adhesion-GPCRs were associated with numerous activities, but their ligands and functions remain unclear. Using unbiased approaches, we observed an unexpected convergence: RTN4 receptors are high-affinity ligands for BAI adhesion-GPCRs. A single thrombospondin type 1-repeat (TSR) domain of BAIs binds to the leucine-rich repeat domain of all three RTN4-receptor isoforms with nanomolar affinity. In the 1.65 Å crystal structure of the BAI1/RTN4-receptor complex, C-mannosylation of tryptophan and O-fucosylation of threonine in the BAI TSR-domains creates a RTN4-receptor/BAI interface shaped by unusual glycoconjugates that enables high-affinity interactions. In human neurons, RTN4 receptors regulate dendritic arborization, axonal elongation, and synapse formation by differential binding to glial versus neuronal BAIs, thereby controlling neural network activity. Thus, BAI binding to RTN4/NoGo receptors represents a receptor-ligand axis that, enabled by rare post-translational modifications, controls development of synaptic circuits.
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•RTN4/NoGo receptors engage in high-affinity interactions with BAI adhesion-GPCRs•RTN4/NoGo receptors bind to BAIs via a glycan-mediated interface•In neurons, interactions of RTN4Rs and BAIs control synapse and dendrite formation•Additionally, interactions of neuronal RTN4Rs with glial BAIs constrain axon growth
RTN4Rs, surface proteins expressed in neurons, interact with BAI adhesion-GPCRs located in either neurons or glia via a glycan-mediated interface, and this interaction regulates the dendritic arborization, axonal elongation, and formation of synapses in cultured human neurons. |
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| AbstractList | RTN4-binding proteins were widely studied as “NoGo” receptors, but their physiological interactors and roles remain elusive. Similarly, BAI adhesion-GPCRs were associated with numerous activities, but their ligands and functions remain unclear. Using unbiased approaches, we observed an unexpected convergence: RTN4 receptors are high-affinity ligands for BAI adhesion-GPCRs. A single thrombospondin type 1-repeat (TSR) domain of BAIs binds to the leucine-rich repeat domain of all three RTN4-receptor isoforms with nanomolar affinity. In the 1.65 Å crystal structure of the BAI1/RTN4-receptor complex, C-mannosylation of tryptophan and O-fucosylation of threonine in the BAI TSR-domains creates a RTN4-receptor/BAI interface shaped by unusual glycoconjugates that enables high-affinity interactions. In human neurons, RTN4 receptors regulate dendritic arborization, axonal elongation, and synapse formation by differential binding to glial versus neuronal BAIs, thereby controlling neural network activity. Thus, BAI binding to RTN4/NoGo receptors represents a receptor-ligand axis that, enabled by rare post-translational modifications, controls development of synaptic circuits.
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•RTN4/NoGo receptors engage in high-affinity interactions with BAI adhesion-GPCRs•RTN4/NoGo receptors bind to BAIs via a glycan-mediated interface•In neurons, interactions of RTN4Rs and BAIs control synapse and dendrite formation•Additionally, interactions of neuronal RTN4Rs with glial BAIs constrain axon growth
RTN4Rs, surface proteins expressed in neurons, interact with BAI adhesion-GPCRs located in either neurons or glia via a glycan-mediated interface, and this interaction regulates the dendritic arborization, axonal elongation, and formation of synapses in cultured human neurons. RTN4-binding proteins were widely studied as “NoGo” receptors, but their physiological interactors and roles remain elusive. Similarly, BAI adhesion-GPCRs were associated with numerous activities, but their ligands and functions remain unclear. Using unbiased approaches, we observed an unexpected convergence: RTN4 receptors are high-affinity ligands for BAI adhesion-GPCRs. A single thrombospondin type 1-repeat (TSR) domain of BAIs binds to the leucine-rich repeat domain of all three RTN4-receptor isoforms with nanomolar affinity. In the 1.65 Å crystal structure of the BAI1/RTN4-receptor complex, C-mannosylation of tryptophan and O-fucosylation of threonine in the BAI TSR-domains creates a RTN4-receptor/BAI interface shaped by unusual glycoconjugates that enables high-affinity interactions. In human neurons, RTN4 receptors regulate dendritic arborization, axonal elongation, and synapse formation by differential binding to glial versus neuronal BAIs, thereby controlling neural network activity. Thus, BAI binding to RTN4/NoGo receptors represents a receptor-ligand axis that, enabled by rare post-translational modifications, controls development of synaptic circuits. RTN4-binding proteins were widely studied as "NoGo" receptors, but their physiological interactors and roles remain elusive. Similarly, BAI adhesion-GPCRs were associated with numerous activities, but their ligands and functions remain unclear. Using unbiased approaches, we observed an unexpected convergence: RTN4 receptors are high-affinity ligands for BAI adhesion-GPCRs. A single thrombospondin type 1-repeat (TSR) domain of BAIs binds to the leucine-rich repeat domain of all three RTN4-receptor isoforms with nanomolar affinity. In the 1.65 Å crystal structure of the BAI1/RTN4-receptor complex, C-mannosylation of tryptophan and O-fucosylation of threonine in the BAI TSR-domains creates a RTN4-receptor/BAI interface shaped by unusual glycoconjugates that enables high-affinity interactions. In human neurons, RTN4 receptors regulate dendritic arborization, axonal elongation, and synapse formation by differential binding to glial versus neuronal BAIs, thereby controlling neural network activity. Thus, BAI binding to RTN4/NoGo receptors represents a receptor-ligand axis that, enabled by rare post-translational modifications, controls development of synaptic circuits.RTN4-binding proteins were widely studied as "NoGo" receptors, but their physiological interactors and roles remain elusive. Similarly, BAI adhesion-GPCRs were associated with numerous activities, but their ligands and functions remain unclear. Using unbiased approaches, we observed an unexpected convergence: RTN4 receptors are high-affinity ligands for BAI adhesion-GPCRs. A single thrombospondin type 1-repeat (TSR) domain of BAIs binds to the leucine-rich repeat domain of all three RTN4-receptor isoforms with nanomolar affinity. In the 1.65 Å crystal structure of the BAI1/RTN4-receptor complex, C-mannosylation of tryptophan and O-fucosylation of threonine in the BAI TSR-domains creates a RTN4-receptor/BAI interface shaped by unusual glycoconjugates that enables high-affinity interactions. In human neurons, RTN4 receptors regulate dendritic arborization, axonal elongation, and synapse formation by differential binding to glial versus neuronal BAIs, thereby controlling neural network activity. Thus, BAI binding to RTN4/NoGo receptors represents a receptor-ligand axis that, enabled by rare post-translational modifications, controls development of synaptic circuits. RTN4-binding proteins were widely studied as "NoGo" receptors, but their physiological interactors and roles remain elusive. Similarly, BAI adhesion-GPCRs were associated with numerous activities, but their ligands and functions remain unclear. Using unbiased approaches, we observed an unexpected convergence: RTN4 receptors are high-affinity ligands for BAI adhesion-GPCRs. A single thrombospondin type 1-repeat (TSR) domain of BAIs binds to the leucine-rich repeat domain of all three RTN4-receptor isoforms with nanomolar affinity. In the 1.65 Å crystal structure of the BAI1/RTN4-receptor complex, C-mannosylation of tryptophan and O-fucosylation of threonine in the BAI TSR-domains creates a RTN4-receptor/BAI interface shaped by unusual glycoconjugates that enables high-affinity interactions. In human neurons, RTN4 receptors regulate dendritic arborization, axonal elongation, and synapse formation by differential binding to glial versus neuronal BAIs, thereby controlling neural network activity. Thus, BAI binding to RTN4/NoGo receptors represents a receptor-ligand axis that, enabled by rare post-translational modifications, controls development of synaptic circuits. RTN4-binding proteins were widely studied as ‘NoGo’ receptors, but their physiological interactors and roles remain elusive. Similarly, BAI adhesion-GPCRs were associated with numerous activities, but their ligands and functions remain unclear. Using unbiased approaches, we observed an unexpected convergence: RTN4-receptors are high-affinity ligands for BAI adhesion-GPCRs. A single thrombospondin type 1-repeat (TSR) domain of BAIs binds to the leucine-rich repeat domain of all three RTN4-receptor isoforms with nanomolar affinity. In the 1.65 Å crystal structure of the BAI1/RTN4-receptor complex, C-mannosylation of tryptophan and O-fucosylation of threonine in the BAI TSR-domains creates a RTN4-receptor/BAI interface shaped by unusual glycoconjugates that enables high-affinity interactions. In human neurons, RTN4-receptors regulate dendritic arborization, axonal elongation and synapse formation by differential binding to glial vs. neuronal BAIs, thereby controlling neural network activity. Thus, BAI-binding to RTN4/NoGo-receptors represents a receptor-ligand axis that, enabled by rare post-translational modifications, controls development of synaptic circuits. RTN4Rs, surface proteins expressed in neurons, interact with BAI adhesion-GPCRs located in either neurons or glia via a glycan-mediated interface, and this interaction regulates the dendritic arborization, axonal elongation and formation of synapses in cultured human neurons. |
| Author | Miao, Yi Wernig, Marius Garcia, K. Christopher Südhof, Thomas C. Wicklein, Rebecca Wang, Jinzhao Fernandes, Ricardo A. Merrill, Sean A. Sun, Zijun Jude, Kevin M. Wang, Jie |
| AuthorAffiliation | 4 Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA 2 Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305, USA 3 Institute for Stem Cell Biology and Regenerative Medicine, Department of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA 6 Lead contact 5 These authors contributed equally 1 Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA |
| AuthorAffiliation_xml | – name: 1 Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA – name: 4 Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA – name: 6 Lead contact – name: 2 Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305, USA – name: 3 Institute for Stem Cell Biology and Regenerative Medicine, Department of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA – name: 5 These authors contributed equally |
| Author_xml | – sequence: 1 givenname: Jie surname: Wang fullname: Wang, Jie organization: Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA – sequence: 2 givenname: Yi surname: Miao fullname: Miao, Yi organization: Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA – sequence: 3 givenname: Rebecca orcidid: 0000-0002-6661-6081 surname: Wicklein fullname: Wicklein, Rebecca organization: Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA – sequence: 4 givenname: Zijun orcidid: 0000-0001-5386-5495 surname: Sun fullname: Sun, Zijun organization: Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA – sequence: 5 givenname: Jinzhao orcidid: 0000-0002-7260-0676 surname: Wang fullname: Wang, Jinzhao organization: Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA – sequence: 6 givenname: Kevin M. orcidid: 0000-0002-3675-5136 surname: Jude fullname: Jude, Kevin M. organization: Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA – sequence: 7 givenname: Ricardo A. surname: Fernandes fullname: Fernandes, Ricardo A. organization: Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA – sequence: 8 givenname: Sean A. orcidid: 0000-0001-5413-4934 surname: Merrill fullname: Merrill, Sean A. organization: Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA – sequence: 9 givenname: Marius surname: Wernig fullname: Wernig, Marius organization: Institute for Stem Cell Biology and Regenerative Medicine, Department of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA – sequence: 10 givenname: K. Christopher surname: Garcia fullname: Garcia, K. Christopher email: kcgarcia@stanford.edu organization: Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA – sequence: 11 givenname: Thomas C. surname: Südhof fullname: Südhof, Thomas C. email: tcs1@stanford.edu organization: Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA |
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| Keywords | RTN4R O-fucosylation C-mannosylation morphology NoGo receptor adhesion-GPCR BAI neuronal network activity synaptic transmission human neuron synapse formation |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 AC02-76SF00515 USDOE Office of Science (SC), Biological and Environmental Research (BER) Author Contributions: Jie W., Y.M., K.C.G., and T.C.S. conceived and designed the study. Jie W. and Y.M. jointly performed the ligand screening, biochemical, structural and functional studies. R.W. identified the BAI-RTN4R interaction in adhesion assays, Z.S. and Jinzhao W. performed the Ca2+-imaging and electrophysiological experiments, respectively, K.M.J., R.A.F. and S.A.M. contributed technically, and M.W. supervised Jinzhao W. Jie W., Y.M., K.C.G. and T.C.S. analyzed the data and wrote the manuscript with input from all authors. |
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| Snippet | RTN4-binding proteins were widely studied as “NoGo” receptors, but their physiological interactors and roles remain elusive. Similarly, BAI adhesion-GPCRs were... RTN4-binding proteins were widely studied as "NoGo" receptors, but their physiological interactors and roles remain elusive. Similarly, BAI adhesion-GPCRs were... RTN4-binding proteins were widely studied as ‘NoGo’ receptors, but their physiological interactors and roles remain elusive. Similarly, BAI adhesion-GPCRs were... |
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| SubjectTerms | adhesion-GPCR Adipokines - metabolism Amino Acid Sequence Angiogenesis Inhibitors - metabolism Animals Axons - metabolism BAI Brain - metabolism C-mannosylation Cell Adhesion Cell Adhesion Molecules, Neuronal - metabolism Complement C1q - metabolism crystal structure Dendrites - metabolism glycoconjugates Glycosylation HEK293 Cells Human Embryonic Stem Cells - metabolism human neuron Humans Ligands Mice Mice, Inbred C57BL morphology Nerve Net - metabolism Neurogenesis neuronal network activity neurons Neurons - metabolism Nogo Proteins - metabolism NoGo receptor Nogo Receptors - metabolism O-fucosylation Polysaccharides - metabolism Protein Binding Protein Domains Receptors, G-Protein-Coupled - metabolism RTN4R Sequence Deletion synapse synapse formation Synapses - metabolism synaptic transmission Synaptic Transmission - physiology threonine tryptophan |
| Title | RTN4/NoGo-receptor binding to BAI adhesion-GPCRs regulates neuronal development |
| URI | https://dx.doi.org/10.1016/j.cell.2021.10.016 https://www.ncbi.nlm.nih.gov/pubmed/34758294 https://www.proquest.com/docview/2596456629 https://www.proquest.com/docview/2636771202 https://www.osti.gov/biblio/1868705 https://pubmed.ncbi.nlm.nih.gov/PMC8620742 |
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