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Structural basis for integration of GluD receptors within synaptic organizer complexes

by Shanks, Natalie F. , Miura, Eriko , Clay, Jordan E. , Siebold, Christian , Behiels, Ester , Greger, Ingo H. , Yuzaki, Michisuke , Matsuda, Keiko , Rossmann, Maxim , Aricescu, A. Radu , Elegheert, Jonathan , Kakegawa, Wataru , Mitakidis, Nikolaos , Motohashi, Junko , Nakagawa, Terunaga , Kohda, Kazuhisa , Chang, Veronica T.

in Animals / Cognitive ability / Fragments / Functional analysis / Glutamates / Ligands / Long-Term Synaptic Depression / Mathematical models / Mice / Nerve Tissue Proteins - chemistry / Nerve Tissue Proteins - metabolism / Neurogenesis / Protein Multimerization / Protein Precursors - chemistry / Protein Precursors - metabolism / Protein Structure, Tertiary / Purkinje Cells - metabolism / Purkinje Cells - physiology / Receptors / Receptors, Glutamate - chemistry / Receptors, Glutamate - metabolism / Signal Transduction / Synapses / Synapses - metabolism / Synapses - physiology

2016

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Structural basis for integration of GluD receptors within synaptic organizer complexes

2016

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Structural basis for integration of GluD receptors within synaptic organizer complexes

2016

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Journal Article

Structural basis for integration of GluD receptors within synaptic organizer complexes

Shanks, Natalie F.,

Miura, Eriko,

Clay, Jordan E.,

Siebold, Christian,

Behiels, Ester,

Greger, Ingo H.,

Yuzaki, Michisuke,

Matsuda, Keiko,

Rossmann, Maxim,

Aricescu, A. Radu,

Elegheert, Jonathan,

Kakegawa, Wataru,

Mitakidis, Nikolaos,

Motohashi, Junko,

Nakagawa, Terunaga,

Kohda, Kazuhisa,

Chang, Veronica T.

2016

Overview

Ionotropic glutamate receptor (iGIuR) family members are integrated into supramolecular complexes that modulate their location and function at excitatory synapses. However, a lack of structural information beyond isolated receptors or fragments thereof currently limits the mechanistic understanding of physiological iGIuR signaling. Here, we report structural and functional analyses of the prototypical molecular bridge linking postsynaptic iGIuR δ2 (GIuD2) and presynaptic β-neurexin 1 (β-NRX1) via CbIn1, a C1q-like synaptic organizer. We show how CbIn1 hexamers \"anchor\" GIuD2 amino-terminal domain dimers to monomeric β-NRX1. This arrangement promotes synaptogenesis and is essential for D-serine–dependent GIuD2 signaling in vivo, which underlies long-term depression of cerebellar parallel fiber–Purkinje cell (PF-PC) synapses and motor coordination in developing mice. These results lead to a model where protein and small-molecule ligands synergistically control synaptic iGIuR function.

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Publisher

American Association for the Advancement of Science,The American Association for the Advancement of Science

Subject

Animals

/ Cognitive ability

/ Fragments

/ Functional analysis

/ Glutamates

/ Ligands

/ Long-Term Synaptic Depression