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

Erscheinungsjahr:

2024

Erschienen:

2024

Enthalten in:

Zur Gesamtaufnahme - volume:43

Enthalten in:

Cell reports - 43(2024), 2 vom: 27. Feb., Seite 113798

Sprache:

Englisch

Beteiligte Personen:

Osaka, Jiro [VerfasserIn]
Ishii, Arisa [VerfasserIn]
Wang, Xu [VerfasserIn]
Iwanaga, Riku [VerfasserIn]
Kawamura, Hinata [VerfasserIn]
Akino, Shogo [VerfasserIn]
Sugie, Atsushi [VerfasserIn]
Hakeda-Suzuki, Satoko [VerfasserIn]
Suzuki, Takashi [VerfasserIn]

Links:

Volltext

Themen:

Beat and Side proteins
CP: Immunology
CP: Neuroscience
Cell-surface proteins
Drosophila visual system
Dsyd-1-Liprin-α
Immunoglobulins
Irre cell recognition module
Journal Article
Membrane Proteins
Subcellular localization
Synapse formation
Synaptic specificity
Transmembrane receptor clustering

Anmerkungen:

Date Completed 04.03.2024

Date Revised 04.03.2024

published: Print-Electronic

Citation Status MEDLINE

doi:

10.1016/j.celrep.2024.113798

funding:

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM368716325