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1. Synapse Formation and Function Across Species: Ancient Roles for CCP, CUB, and TSP-1 Structural Domains

Author

Inés González-Calvo, Mélissa Cizeron, Jean-Louis Bessereau, and Fekrije Selimi

Subjects
synapse, molecular conservation, CCP, CUB, TSP-1, invertebrates, Neurosciences. Biological psychiatry. Neuropsychiatry, RC321-571
Abstract

The appearance of synapses was a crucial step in the creation of the variety of nervous systems that are found in the animal kingdom. With increased complexity of the organisms came a greater number of synaptic proteins. In this review we describe synaptic proteins that contain the structural domains CUB, CCP, or TSP-1. These domains are found in invertebrates and vertebrates, and CUB and CCP domains were initially described in proteins belonging to the complement system of innate immunity. Interestingly, they are found in synapses of the nematode C. elegans, which does not have a complement system, suggesting an ancient function. Comparison of the roles of CUB-, CCP-, and TSP-1 containing synaptic proteins in various species shows that in more complex nervous systems, these structural domains are combined with other domains and that there is partial conservation of their function. These three domains are thus basic building blocks of the synaptic architecture. Further studies of structural domains characteristic of synaptic proteins in invertebrates such as C. elegans and comparison of their role in mammals will help identify other conserved synaptic molecular building blocks. Furthermore, this type of functional comparison across species will also identify structural domains added during evolution in correlation with increased complexity, shedding light on mechanisms underlying cognition and brain diseases.

Published
2022
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2. Sushi domain-containing protein 4 controls synaptic plasticity and motor learning

Author

Inés González-Calvo, Keerthana Iyer, Mélanie Carquin, Anouar Khayachi, Fernando A Giuliani, Séverine M Sigoillot, Jean Vincent, Martial Séveno, Maxime Veleanu, Sylvana Tahraoui, Mélanie Albert, Oana Vigy, Célia Bosso-Lefèvre, Yann Nadjar, Andréa Dumoulin, Antoine Triller, Jean-Louis Bessereau, Laure Rondi-Reig, Philippe Isope, and Fekrije Selimi

Subjects
synapse, plasticity, cerebellum, proteostasis, Medicine, Science, Biology (General), QH301-705.5
Abstract

Fine control of protein stoichiometry at synapses underlies brain function and plasticity. How proteostasis is controlled independently for each type of synaptic protein in a synapse-specific and activity-dependent manner remains unclear. Here, we show that Susd4, a gene coding for a complement-related transmembrane protein, is expressed by many neuronal populations starting at the time of synapse formation. Constitutive loss-of-function of Susd4 in the mouse impairs motor coordination adaptation and learning, prevents long-term depression at cerebellar synapses, and leads to misregulation of activity-dependent AMPA receptor subunit GluA2 degradation. We identified several proteins with known roles in the regulation of AMPA receptor turnover, in particular ubiquitin ligases of the NEDD4 subfamily, as SUSD4 binding partners. Our findings shed light on the potential role of SUSD4 mutations in neurodevelopmental diseases.

Published
2021
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3. The Secreted Protein C1QL1 and Its Receptor BAI3 Control the Synaptic Connectivity of Excitatory Inputs Converging on Cerebellar Purkinje Cells

Author

Séverine M. Sigoillot, Keerthana Iyer, Francesca Binda, Inés González-Calvo, Maëva Talleur, Guilan Vodjdani, Philippe Isope, and Fekrije Selimi

Subjects
Biology (General), QH301-705.5
Abstract

Precise patterns of connectivity are established by different types of afferents on a given target neuron, leading to well-defined and non-overlapping synaptic territories. What regulates the specific characteristics of each type of synapse, in terms of number, morphology, and subcellular localization, remains to be understood. Here, we show that the signaling pathway formed by the secreted complement C1Q-related protein C1QL1 and its receptor, the adhesion-GPCR brain angiogenesis inhibitor 3 (BAI3), controls the stereotyped pattern of connectivity established by excitatory afferents on cerebellar Purkinje cells. The BAI3 receptor modulates synaptogenesis of both parallel fiber and climbing fiber afferents. The restricted and timely expression of its ligand C1QL1 in inferior olivary neurons ensures the establishment of the proper synaptic territory for climbing fibers. Given the broad expression of C1QL and BAI proteins in the developing mouse brain, our study reveals a general mechanism contributing to the formation of a functional brain.

Published
2015
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4. Sushi domain-containing protein 4 controls synaptic plasticity and motor learning

Author

Keerthana Iyer, Fernando A Giuliani, Laure Rondi-Reig, Philippe Isope, Yann Nadjar, Antoine Triller, Jean-Louis Bessereau, Mélanie Albert, Andréa Dumoulin, Séverine M. Sigoillot, Oana Vigy, Maxime Veleanu, Jean Vincent, Mélanie Carquin, Anouar Khayachi, Célia Bosso-Lefèvre, Martial Séveno, Fekrije Selimi, Inés González-Calvo, Sylvana Tahraoui, Centre interdisciplinaire de recherche en biologie (CIRB), Labex MemoLife, École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Collège de France (CdF (institution))-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut des Neurosciences Cellulaires et Intégratives (INCI), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Institut de Biologie Paris Seine (IBPS), Sorbonne Université (SU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), BioCampus Montpellier (BCM), Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie de l'ENS Paris (IBENS), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Département de Biologie - ENS Paris, Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut NeuroMyoGène (INMG), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-École normale supérieure - Paris (ENS-PSL), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Neuroscience Paris Seine (NPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), CeZaMe - Cervelet, navigation et mémoire = Memory, Navigation and Aging (NPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Paris Seine (IBPS), BioCampus (BCM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Département de Biologie - ENS Paris, Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Gestionnaire, Hal Sorbonne Université, Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-Collège de France (CdF (institution))-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Collège de France (CdF (institution))-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de biologie de l'ENS Paris (UMR 8197/1024) (IBENS), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-École normale supérieure - Paris (ENS Paris), and Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Male, 0301 basic medicine, Sushi domain, cerebellum, QH301-705.5, Science, [SDV]Life Sciences [q-bio], Protein subunit, AMPA receptor, Motor Activity, General Biochemistry, Genetics and Molecular Biology, neuroscience, Synapse, Mice, 03 medical and health sciences, 0302 clinical medicine, Ubiquitin, synapse, Animals, Learning, Biology (General), mouse, Complement Inactivator Proteins, Neuronal Plasticity, proteostasis, General Immunology and Microbiology, biology, General Neuroscience, Membrane Proteins, General Medicine, Transmembrane protein, [SDV] Life Sciences [q-bio], 030104 developmental biology, Proteostasis, plasticity, Synaptic plasticity, biology.protein, Medicine, Neuroscience, 030217 neurology & neurosurgery, Research Article
Abstract

Fine control of protein stoichiometry at synapses underlies brain function and plasticity. How proteostasis is controlled independently for each type of synaptic protein in a synapse-specific and activity-dependent manner remains unclear. Here, we show that Susd4, a gene coding for a complement-related transmembrane protein, is expressed by many neuronal populations starting at the time of synapse formation. Constitutive loss-of-function of Susd4 in the mouse impairs motor coordination adaptation and learning, prevents long-term depression at cerebellar synapses, and leads to misregulation of activity-dependent AMPA receptor subunit GluA2 degradation. We identified several proteins with known roles in the regulation of AMPA receptor turnover, in particular ubiquitin ligases of the NEDD4 subfamily, as SUSD4 binding partners. Our findings shed light on the potential role of SUSD4 mutations in neurodevelopmental diseases.

Published
2021

5. Author response: Sushi domain-containing protein 4 controls synaptic plasticity and motor learning

Author

Célia Bosso-Lefèvre, Oana Vigy, Jean Vincent, Fernando A Giuliani, Jean-Louis Bessereau, Mélanie Carquin, Maxime Veleanu, Antoine Triller, Anouar Khayachi, Inés González-Calvo, Sylvana Tahraoui, Keerthana Iyer, Laure Rondi-Reig, Philippe Isope, Andréa Dumoulin, Yann Nadjar, Mélanie Albert, Séverine M. Sigoillot, Martial Séveno, and Fekrije Selimi

Subjects
Sushi domain, Synaptic plasticity, Biology, Motor learning, Neuroscience
Published
2021

6. Expression and role of Galectin-3 in the postnatal development of the cerebellum

Author

Inés González-Calvo, Fekrije Selimi, Centre interdisciplinaire de recherche en biologie (CIRB), Labex MemoLife, École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Collège de France (CdF (institution))-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-École normale supérieure - Paris (ENS Paris), and Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
0303 health sciences, Cerebellum, [SDV]Life Sciences [q-bio], Purkinje cell, Neurogenesis, Synaptogenesis, Biology, 03 medical and health sciences, 0302 clinical medicine, medicine.anatomical_structure, nervous system, Cerebellar cortex, Synaptic plasticity, medicine, Choroid plexus, Axon guidance, Neuroscience, 030217 neurology & neurosurgery, 030304 developmental biology
Abstract

Many proteins initially identified in the immune system play roles in neurogenesis, neuronal migration, axon guidance, synaptic plasticity and other processes related to the formation and refinement of neural circuits. Although the function of the immune-related protein Galectin-3 (LGALS3) has been extensively studied in the regulation of inflammation, cancer and microglia activation, little is known about its role in the development of the brain. In this study, we identified that LGALS3 is expressed in the developing postnatal cerebellum. More precisely, LGALS3 is expressed by cells in meninges and in the choroid plexus, and in subpopulations of astrocytes and of microglial cells in the cerebellar cortex. Analysis ofLgals3knockout mice showed thatLgals3is dispensable for the development of cerebellar cytoarchitecture and Purkinje cell excitatory synaptogenesis in the mouse.

Published
2019

7. SUSD4 Controls Activity-Dependent Degradation of AMPA Receptor GLUA2 and Synaptic Plasticity

Author

Philippe Isope, Oana Vigy, Célia Bosso-Lefèvre, Andréa Dumoulin, Mélanie Albert, Fernando A Giuliani, Jean-Louis Bessereau, Inés González-Calvo, Sylvana Tahraoui, Séverine M. Sigoillot, Anouar Khayachi, Maxime Veleanu, Mélanie Carquin, Keerthana Iyer, Yann Nadjar, Martial Séveno, Laure Rondi-Reig, Antoine Triller, Fekrije Selimi, and Jean Vincent

Subjects
0303 health sciences, biology, Protein subunit, NEDD4, AMPA receptor, Transmembrane protein, Motor coordination, 03 medical and health sciences, 0302 clinical medicine, Proteostasis, Ubiquitin, Synaptic plasticity, biology.protein, Neuroscience, 030217 neurology & neurosurgery, 030304 developmental biology
Abstract

SummaryAt excitatory synapses, the choice between recycling or degradation of glutamate AMPA receptors controls the direction of synaptic plasticity. In this context, how the degradation machinery is targeted to specific synaptic substrates in an activity-dependent manner is not understood. Here we show that SUSD4, a complement-related transmembrane protein, is a tether for HECT ubiquitin ligases of the NEDD4 subfamily, which promote the degradation of a large number of cellular substrates. SUSD4 is expressed by many neuronal populations starting at the time of synapse formation. Loss-of-function ofSusd4in the mouse prevents activity-dependent degradation of the GLUA2 AMPA receptor subunit and long-term depression at cerebellar synapses, and leads to impairment in motor coordination adaptation and learning. SUSD4 could thus act as an adaptor targeting NEDD4 ubiquitin ligases to AMPA receptors during long-term synaptic plasticity. These findings shed light on the potential contribution ofSUSD4mutations to the etiology of neurodevelopmental diseases.

Published
2019
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8. The secreted protein C1QL1 and its receptor BAI3 control the synaptic connectivity of excitatory inputs converging on cerebellar Purkinje cells

Author

Keerthana Iyer, Guilan Vodjdani, Inés González-Calvo, Philippe Isope, Maëva Talleur, Séverine M. Sigoillot, Fekrije Selimi, Francesca Binda, Centre interdisciplinaire de recherche en biologie (CIRB), Labex MemoLife, École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Collège de France (CdF (institution))-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Département Neurotransmission et sécrétion neuroendocrine, Centre National de la Recherche Scientifique (CNRS), Neuroprotection du Cerveau en Développement / Promoting Research Oriented Towards Early Cns Therapies (PROTECT), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Robert Debré-Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), This work has received support under the program « Investissements d’Avenir » launched by the French Government and implemented by the ANR, with the references: ANR-10-LABX-54 MEMO LIFE (SS, FS) and ANR-11-IDEX-0001-02 PSL* Research University (IGC, FS), and under the TIGER project funded by INTERREG IV Rhin Supérieur program and European Funds for Regional Development (FEDER, # A31, FB and PI). Funding was also provided by Fondation Bettencourt Schuller, CNRS, NeRF Ile de France (SS), Ecole des Neurosciences de Paris (KI), Fondation pour la Recherche Médicale (MT), ATIP AVENIR (FS), Fondation Jérôme Lejeune (FS), Association Française pour le Syndrôme de Rett (FS), ANR-2010-JCJC-1403-1 (PI), ANR-13-SAMA-0010-01 (FS)., ANR-11-IDEX-0001,Amidex,INITIATIVE D'EXCELLENCE AIX MARSEILLE UNIVERSITE(2011), ANR-10-IDEX-0001,PSL,Paris Sciences et Lettres(2010), Centre National de la Recherche Scientifique (CNRS) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Collège de France, Université de Strasbourg - Institut des Neurosciences Cellulaires et Intégratives (INCI) - Centre National de la Recherche Scientifique (CNRS), Neuroprotection du Cerveau en Développement (PROTECT), Assistance publique - Hôpitaux de Paris (AP-HP) - Hôpital Robert Debré - Université Paris Diderot - Paris 7 (UP7) - Institut National de la Santé et de la Recherche Médicale (INSERM), ANR-11-IDEX-0001-02, A*MIDEX, Projet Investissements d'Avenir(2012), and ANR-10-LABX-54, MEMO LIFE, Projet Investissements d'Avenir

Subjects
Synaptogenesis, Parallel fiber, Climbing fiber, Anatomy, Biology, General Biochemistry, Genetics and Molecular Biology, Synapse, medicine.anatomical_structure, lcsh:Biology (General), medicine, Excitatory postsynaptic potential, [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Neuron, [SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Signal transduction, Receptor, Neuroscience, lcsh:QH301-705.5
Abstract

International audience; Precise patterns of connectivity are established by different types of afferents on a given target neuron, leading to well-defined and non-overlapping synaptic territories. What regulates the specific characteristics of each type of synapse, in terms of number, morphology and subcellular localization, remains to be understood. Here we show that the signaling pathway formed by the secreted complement C1Q-related protein C1QL1 and its receptor, the adhesion-GPCR Brain Angiogenesis Inhibitor 3 (BAI3), control the stereotyped pattern of connectivity established by excitatory afferents on cerebellar Purkinje cells. The BAI3 receptor modulates synaptogenesis of both parallel fiber and climbing fiber afferents. The restricted and timely expression of its ligand C1QL1 in inferior olivary neurons ensures the establishment of the proper synaptic territory for climbing fibers. Given the broad expression of C1QL and BAI proteins in the developing mouse brain, our study reveals a general mechanism contributing to the formation of a functional brain.

Published
2015

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