Complex formation of immunoglobulin superfamily molecules Side-IV and Beat-IIb regulates synaptic specificity
Copyright © 2024 The Author(s). Published by Elsevier Inc. All rights reserved..
Neurons establish specific synapses based on the adhesive properties of cell-surface proteins while also retaining the ability to form synapses in a relatively non-selective manner. However, comprehensive understanding of the underlying mechanism reconciling these opposing characteristics remains incomplete. Here, we have identified Side-IV/Beat-IIb, members of the Drosophila immunoglobulin superfamily, as a combination of cell-surface recognition molecules inducing synapse formation. The Side-IV/Beat-IIb combination transduces bifurcated signaling with Side-IV's co-receptor, Kirre, and a synaptic scaffold protein, Dsyd-1. Genetic experiments and subcellular protein localization analyses showed the Side-IV/Beat-IIb/Kirre/Dsyd-1 complex to have two essential functions. First, it narrows neuronal binding specificity through Side-IV/Beat-IIb extracellular interactions. Second, it recruits synapse formation factors, Kirre and Dsyd-1, to restrict synaptic loci and inhibit miswiring. This dual function explains how the combinations of cell-surface molecules enable the ranking of preferred interactions among neuronal pairs to achieve synaptic specificity in complex circuits in vivo.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2024 |
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Erschienen: |
2024 |
Enthalten in: |
Zur Gesamtaufnahme - volume:43 |
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Enthalten in: |
Cell reports - 43(2024), 2 vom: 27. Feb., Seite 113798 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Osaka, Jiro [VerfasserIn] |
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Links: |
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Anmerkungen: |
Date Completed 04.03.2024 Date Revised 04.03.2024 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1016/j.celrep.2024.113798 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM368716325 |
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520 | |a Neurons establish specific synapses based on the adhesive properties of cell-surface proteins while also retaining the ability to form synapses in a relatively non-selective manner. However, comprehensive understanding of the underlying mechanism reconciling these opposing characteristics remains incomplete. Here, we have identified Side-IV/Beat-IIb, members of the Drosophila immunoglobulin superfamily, as a combination of cell-surface recognition molecules inducing synapse formation. The Side-IV/Beat-IIb combination transduces bifurcated signaling with Side-IV's co-receptor, Kirre, and a synaptic scaffold protein, Dsyd-1. Genetic experiments and subcellular protein localization analyses showed the Side-IV/Beat-IIb/Kirre/Dsyd-1 complex to have two essential functions. First, it narrows neuronal binding specificity through Side-IV/Beat-IIb extracellular interactions. Second, it recruits synapse formation factors, Kirre and Dsyd-1, to restrict synaptic loci and inhibit miswiring. This dual function explains how the combinations of cell-surface molecules enable the ranking of preferred interactions among neuronal pairs to achieve synaptic specificity in complex circuits in vivo | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Beat and Side proteins | |
650 | 4 | |a CP: Immunology | |
650 | 4 | |a CP: Neuroscience | |
650 | 4 | |a Drosophila visual system | |
650 | 4 | |a Dsyd-1-Liprin-α | |
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650 | 4 | |a irre cell recognition module | |
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650 | 4 | |a synaptic specificity | |
650 | 4 | |a transmembrane receptor clustering | |
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700 | 1 | |a Ishii, Arisa |e verfasserin |4 aut | |
700 | 1 | |a Wang, Xu |e verfasserin |4 aut | |
700 | 1 | |a Iwanaga, Riku |e verfasserin |4 aut | |
700 | 1 | |a Kawamura, Hinata |e verfasserin |4 aut | |
700 | 1 | |a Akino, Shogo |e verfasserin |4 aut | |
700 | 1 | |a Sugie, Atsushi |e verfasserin |4 aut | |
700 | 1 | |a Hakeda-Suzuki, Satoko |e verfasserin |4 aut | |
700 | 1 | |a Suzuki, Takashi |e verfasserin |4 aut | |
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