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Article ; Online: Isolation of Immunocomplexes from Zebrafish Brain.

Michel, Jennifer Carlisle / Miller, Adam C

2023 Volume 13, Issue 7, Page(s) e4646

Abstract: Zebrafish is an excellent model to study vertebrate neurobiology, but its synaptic components that mediate and regulate fast electrical synaptic transmission are largely unidentified. Here, we describe methods to solubilize and immunoprecipitate adult ... ...

Abstract	Zebrafish is an excellent model to study vertebrate neurobiology, but its synaptic components that mediate and regulate fast electrical synaptic transmission are largely unidentified. Here, we describe methods to solubilize and immunoprecipitate adult zebrafish brain homogenate under conditions to preserve electrical synapse protein complexes. The methods presented are well-suited to probe electrical synapse immunocomplexes, and potentially other brain-derived immunocomplexes, for candidate interactors from zebrafish brain.
Language	English
Publishing date	2023-04-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	2833269-6
ISSN	2331-8325 ; 2331-8325
ISSN (online)	2331-8325
ISSN	2331-8325
DOI	10.21769/BioProtoc.4646
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Article ; Online: The

Michel, Jennifer Carlisle / Lasseigne, Abagael M / Marsh, Audrey J / Miller, Adam C

microPublication biology

2022 Volume 2022

Abstract: To investigate electrical synapse ... ...

Abstract	To investigate electrical synapse formation
Language	English
Publishing date	2022-07-03
Publishing country	United States
Document type	Journal Article
ISSN	2578-9430
ISSN (online)	2578-9430
DOI	10.17912/micropub.biology.000593
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Article ; Online: Transformation of an early-established motor circuit during maturation in zebrafish.

Pallucchi, Irene / Bertuzzi, Maria / Michel, Jennifer Carlisle / Miller, Adam C / El Manira, Abdeljabbar

Cell reports

2022 Volume 39, Issue 2, Page(s) 110654

Abstract: Locomotion is mediated by spinal circuits that generate movements with a precise coordination and vigor. The assembly of these circuits is defined early during development; however, whether their organization and function remain invariant throughout ... ...

Abstract	Locomotion is mediated by spinal circuits that generate movements with a precise coordination and vigor. The assembly of these circuits is defined early during development; however, whether their organization and function remain invariant throughout development is unclear. Here, we show that the first established fast circuit between two dorsally located V2a interneuron types and the four primary motoneurons undergoes major transformation in adult zebrafish compared with what was reported in larvae. There is a loss of existing connections and establishment of new connections combined with alterations in the mode, plasticity, and strength of synaptic transmission. In addition, we show that this circuit no longer serves as a swim rhythm generator, but instead its components become embedded within the spinal escape circuit and control propulsion following the initial escape turn. Our results thus reveal significant changes in the organization and function of a motor circuit as animals develop toward adulthood.
MeSH term(s)	Animals ; Interneurons/physiology ; Locomotion/physiology ; Motor Neurons/physiology ; Spinal Cord/physiology ; Zebrafish/physiology
Language	English
Publishing date	2022-04-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2022.110654
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Article ; Online: Neurobeachin controls the asymmetric subcellular distribution of electrical synapse proteins.

Martin, E Anne / Michel, Jennifer Carlisle / Kissinger, Jane S / Echeverry, Fabio A / Lin, Ya-Ping / O'Brien, John / Pereda, Alberto E / Miller, Adam C

Current biology : CB

2023 Volume 33, Issue 10, Page(s) 2063–2074.e4

Abstract: The subcellular positioning of synapses and their specialized molecular compositions form the fundamental basis of neural circuits. Like chemical synapses, electrical synapses are constructed from an assortment of adhesion, scaffolding, and regulatory ... ...

Abstract	The subcellular positioning of synapses and their specialized molecular compositions form the fundamental basis of neural circuits. Like chemical synapses, electrical synapses are constructed from an assortment of adhesion, scaffolding, and regulatory molecules, yet little is known about how these molecules localize to specific neuronal compartments. Here, we investigate the relationship between the autism- and epilepsy-associated gene Neurobeachin, the neuronal gap junction channel-forming Connexins, and the electrical synapse scaffold ZO1. Using the zebrafish Mauthner circuit, we find Neurobeachin localizes to the electrical synapse independently of ZO1 and Connexins. By contrast, we show Neurobeachin is required postsynaptically for the robust localization of ZO1 and Connexins. We demonstrate that Neurobeachin binds ZO1 but not Connexins. Finally, we find Neurobeachin is required to restrict electrical postsynaptic proteins to dendrites, but not electrical presynaptic proteins to axons. Together, the results reveal an expanded understanding of electrical synapse molecular complexity and the hierarchical interactions required to build neuronal gap junctions. Further, these findings provide novel insight into the mechanisms by which neurons compartmentalize the localization of electrical synapse proteins and provide a cell biological mechanism for the subcellular specificity of electrical synapse formation and function.
MeSH term(s)	Animals ; Connexins/metabolism ; Electrical Synapses/physiology ; Gap Junctions/metabolism ; Neurons/physiology ; Synapses/physiology ; Zebrafish/metabolism
Chemical Substances	Connexins ; nbeaa protein, zebrafish
Language	English
Publishing date	2023-05-11
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2023.04.049
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Article ; Online: Electrical synapse structure requires distinct isoforms of a postsynaptic scaffold.

PLoS genetics

2023 Volume 19, Issue 11, Page(s) e1011045

Abstract: Electrical synapses are neuronal gap junction (GJ) channels associated with a macromolecular complex called the electrical synapse density (ESD), which regulates development and dynamically modifies electrical transmission. However, the proteomic makeup ... ...

Abstract	Electrical synapses are neuronal gap junction (GJ) channels associated with a macromolecular complex called the electrical synapse density (ESD), which regulates development and dynamically modifies electrical transmission. However, the proteomic makeup and molecular mechanisms utilized by the ESD that direct electrical synapse formation are not well understood. Using the Mauthner cell of zebrafish as a model, we previously found that the intracellular scaffolding protein ZO1b is a member of the ESD, localizing postsynaptically, where it is required for GJ channel localization, electrical communication, neural network function, and behavior. Here, we show that the complexity of the ESD is further diversified by the genomic structure of the ZO1b gene locus. The ZO1b gene is alternatively initiated at three transcriptional start sites resulting in isoforms with unique N-termini that we call ZO1b-Alpha, -Beta, and -Gamma. We demonstrate that ZO1b-Beta and ZO1b-Gamma are broadly expressed throughout the nervous system and localize to electrical synapses. By contrast, ZO1b-Alpha is expressed mainly non-neuronally and is not found at synapses. We generate mutants in all individual isoforms, as well as double mutant combinations in cis on individual chromosomes, and find that ZO1b-Beta is necessary and sufficient for robust GJ channel localization. ZO1b-Gamma, despite its localization to the synapse, plays an auxiliary role in channel localization. This study expands the notion of molecular complexity at the ESD, revealing that an individual genomic locus can contribute distinct isoforms to the macromolecular complex at electrical synapses. Further, independent scaffold isoforms have differential contributions to developmental assembly of the interneuronal GJ channels. We propose that ESD molecular complexity arises both from the diversity of unique genes and from distinct isoforms encoded by single genes. Overall, ESD proteomic diversity is expected to have critical impacts on the development, structure, function, and plasticity of electrical transmission.
MeSH term(s)	Animals ; Electrical Synapses/physiology ; Zebrafish/genetics ; Proteomics ; Synapses/genetics ; Gap Junctions/physiology ; Ion Channels ; Protein Isoforms/genetics
Chemical Substances	Ion Channels ; Protein Isoforms
Language	English
Publishing date	2023-11-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1011045
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Article ; Online: Electrical synaptic transmission requires a postsynaptic scaffolding protein.

Lasseigne, Abagael M / Echeverry, Fabio A / Ijaz, Sundas / Michel, Jennifer Carlisle / Martin, E Anne / Marsh, Audrey J / Trujillo, Elisa / Marsden, Kurt C / Pereda, Alberto E / Miller, Adam C

eLife

2021 Volume 10

Abstract: Electrical synaptic transmission relies on neuronal gap junctions containing channels constructed by Connexins. While at chemical synapses neurotransmitter-gated ion channels are critically supported by scaffolding proteins, it is unknown if channels at ... ...

Abstract	Electrical synaptic transmission relies on neuronal gap junctions containing channels constructed by Connexins. While at chemical synapses neurotransmitter-gated ion channels are critically supported by scaffolding proteins, it is unknown if channels at electrical synapses require similar scaffold support. Here, we investigated the functional relationship between neuronal Connexins and Zonula Occludens 1 (ZO1), an intracellular scaffolding protein localized to electrical synapses. Using model electrical synapses in zebrafish Mauthner cells, we demonstrated that ZO1 is required for robust synaptic Connexin localization, but Connexins are dispensable for ZO1 localization. Disrupting this hierarchical ZO1/Connexin relationship abolishes electrical transmission and disrupts Mauthner cell-initiated escape responses. We found that ZO1 is asymmetrically localized exclusively postsynaptically at neuronal contacts where it functions to assemble intercellular channels. Thus, forming functional neuronal gap junctions requires a postsynaptic scaffolding protein. The critical function of a scaffolding molecule reveals an unanticipated complexity of molecular and functional organization at electrical synapses.
MeSH term(s)	Animals ; Connexins/metabolism ; Electrical Synapses/physiology ; Synaptic Transmission/genetics ; Zebrafish/genetics ; Zebrafish/physiology ; Zebrafish Proteins/genetics ; Zebrafish Proteins/metabolism ; Zonula Occludens-1 Protein/genetics ; Zonula Occludens-1 Protein/metabolism
Chemical Substances	Connexins ; Zebrafish Proteins ; Zonula Occludens-1 Protein
Language	English
Publishing date	2021-04-28
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.66898
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Article ; Online: Asymmetry of an Intracellular Scaffold at Vertebrate Electrical Synapses.

Marsh, Audrey J / Michel, Jennifer Carlisle / Adke, Anisha P / Heckman, Emily L / Miller, Adam C

Current biology : CB

2017 Volume 27, Issue 22, Page(s) 3561–3567.e4

Abstract: Neuronal synaptic connections are either chemical or electrical, and these two types of synapses work together to dynamically define neural circuit function [1]. Although we know a great deal about the molecules that support chemical synapse formation ... ...

Abstract	Neuronal synaptic connections are either chemical or electrical, and these two types of synapses work together to dynamically define neural circuit function [1]. Although we know a great deal about the molecules that support chemical synapse formation and function, we know little about the macromolecular complexes that regulate electrical synapses. Electrical synapses are created by gap junction (GJ) channels that provide direct ionic communication between neurons [2]. Although they are often molecularly and functionally symmetric, recent work has found that pre- and postsynaptic neurons can contribute different GJ-forming proteins, creating molecularly asymmetric channels that are correlated with functional asymmetry at the synapse [3, 4]. Associated with the GJs are structures observed by electron microscopy termed the electrical synapse density (ESD) [5]. The ESD has been suggested to be critical for the formation and function of the electrical synapse, yet the biochemical makeup of these structures is poorly understood. Here we find that electrical synapse formation in vivo requires an intracellular scaffold called Tight Junction Protein 1b (Tjp1b). Tjp1b is localized to the electrical synapse, where it is required for the stabilization of the GJs and for electrical synapse function. Strikingly, we find that Tjp1b protein localizes and functions asymmetrically, exclusively on the postsynaptic side of the synapse. Our findings support a novel model of electrical synapse molecular asymmetry at the level of an intracellular scaffold that is required for building the electrical synapse. We propose that such ESD asymmetries could be used by all nervous systems to support molecular and functional asymmetries at electrical synapses.
MeSH term(s)	Animals ; Connexins/metabolism ; Electrical Synapses/physiology ; Gap Junctions/metabolism ; Ion Channels/metabolism ; Nervous System ; Neurons/physiology ; Synapses/physiology ; Tight Junctions/metabolism ; Tight Junctions/physiology ; Vertebrates/metabolism ; Zebrafish/growth & development ; Zebrafish/physiology ; Zebrafish Proteins/metabolism ; Zonula Occludens-1 Protein/metabolism ; Zonula Occludens-1 Protein/physiology
Chemical Substances	Connexins ; Ion Channels ; Zebrafish Proteins ; Zonula Occludens-1 Protein
Language	English
Publishing date	2017-11-02
Publishing country	England
Document type	Journal Article
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2017.10.011
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Article ; Online: Crystal structure of the ATP-gated P2X(4) ion channel in the closed state.

Kawate, Toshimitsu / Michel, Jennifer Carlisle / Birdsong, William T / Gouaux, Eric

Nature

2009 Volume 460, Issue 7255, Page(s) 592–598

Abstract: P2X receptors are cation-selective ion channels gated by extracellular ATP, and are implicated in diverse physiological processes, from synaptic transmission to inflammation to the sensing of taste and pain. Because P2X receptors are not related to other ...

Abstract	P2X receptors are cation-selective ion channels gated by extracellular ATP, and are implicated in diverse physiological processes, from synaptic transmission to inflammation to the sensing of taste and pain. Because P2X receptors are not related to other ion channel proteins of known structure, there is at present no molecular foundation for mechanisms of ligand-gating, allosteric modulation and ion permeation. Here we present crystal structures of the zebrafish P2X(4) receptor in its closed, resting state. The chalice-shaped, trimeric receptor is knit together by subunit-subunit contacts implicated in ion channel gating and receptor assembly. Extracellular domains, rich in beta-strands, have large acidic patches that may attract cations, through fenestrations, to vestibules near the ion channel. In the transmembrane pore, the 'gate' is defined by an approximately 8 A slab of protein. We define the location of three non-canonical, intersubunit ATP-binding sites, and suggest that ATP binding promotes subunit rearrangement and ion channel opening.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Animals ; Binding Sites ; Cell Line ; Crystallography, X-Ray ; Gadolinium/metabolism ; Humans ; Ion Channels/antagonists & inhibitors ; Ion Channels/chemistry ; Membrane Proteins/chemistry ; Models, Molecular ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; Purinergic P2 Receptor Antagonists ; Receptors, Purinergic P2/chemistry ; Receptors, Purinergic P2X4 ; Zebrafish/physiology ; Zebrafish Proteins/antagonists & inhibitors ; Zebrafish Proteins/chemistry
Chemical Substances	Ion Channels ; Membrane Proteins ; P2RX4 protein, human ; Purinergic P2 Receptor Antagonists ; Receptors, Purinergic P2 ; Receptors, Purinergic P2X4 ; Zebrafish Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; Gadolinium (AU0V1LM3JT)
Language	English
Publishing date	2009-07-30
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/nature08198
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Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 9: Show issues
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Article ; Online: NMDA receptor structures reveal subunit arrangement and pore architecture.

Lee, Chia-Hsueh / Lü, Wei / Michel, Jennifer Carlisle / Goehring, April / Du, Juan / Song, Xianqiang / Gouaux, Eric

Nature

2014 Volume 511, Issue 7508, Page(s) 191–197

Abstract: N-methyl-d-aspartate (NMDA) receptors are Hebbian-like coincidence detectors, requiring binding of glycine and glutamate in combination with the relief of voltage-dependent magnesium block to open an ion conductive pore across the membrane bilayer. ... ...

Abstract	N-methyl-d-aspartate (NMDA) receptors are Hebbian-like coincidence detectors, requiring binding of glycine and glutamate in combination with the relief of voltage-dependent magnesium block to open an ion conductive pore across the membrane bilayer. Despite the importance of the NMDA receptor in the development and function of the brain, a molecular structure of an intact receptor has remained elusive. Here we present X-ray crystal structures of the Xenopus laevis GluN1-GluN2B NMDA receptor with the allosteric inhibitor, Ro25-6981, partial agonists and the ion channel blocker, MK-801. Receptor subunits are arranged in a 1-2-1-2 fashion, demonstrating extensive interactions between the amino-terminal and ligand-binding domains. The transmembrane domains harbour a closed-blocked ion channel, a pyramidal central vestibule lined by residues implicated in binding ion channel blockers and magnesium, and a ∼twofold symmetric arrangement of ion channel pore loops. These structures provide new insights into the architecture, allosteric coupling and ion channel function of NMDA receptors.
MeSH term(s)	Animals ; Dizocilpine Maleate/chemistry ; Ion Channels/chemistry ; Ligands ; Models, Molecular ; Phenols ; Piperidines/chemistry ; Protein Binding ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Receptors, N-Methyl-D-Aspartate/chemistry ; Xenopus laevis/physiology
Chemical Substances	Ion Channels ; Ligands ; Phenols ; Piperidines ; Protein Subunits ; Receptors, N-Methyl-D-Aspartate ; Ro 25-6981 ; Dizocilpine Maleate (6LR8C1B66Q)
Language	English
Publishing date	2014-06-22
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/nature13548
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Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Screening and large-scale expression of membrane proteins in mammalian cells for structural studies.

Goehring, April / Lee, Chia-Hsueh / Wang, Kevin H / Michel, Jennifer Carlisle / Claxton, Derek P / Baconguis, Isabelle / Althoff, Thorsten / Fischer, Suzanne / Garcia, K Christopher / Gouaux, Eric

Nature protocols

2014 Volume 9, Issue 11, Page(s) 2574–2585

Abstract: Structural, biochemical and biophysical studies of eukaryotic membrane proteins are often hampered by difficulties in overexpression of the candidate molecule. Baculovirus transduction of mammalian cells (BacMam), although a powerful method to ... ...

Abstract	Structural, biochemical and biophysical studies of eukaryotic membrane proteins are often hampered by difficulties in overexpression of the candidate molecule. Baculovirus transduction of mammalian cells (BacMam), although a powerful method to heterologously express membrane proteins, can be cumbersome for screening and expression of multiple constructs. We therefore developed plasmid Eric Gouaux (pEG) BacMam, a vector optimized for use in screening assays, as well as for efficient production of baculovirus and robust expression of the target protein. In this protocol, we show how to use small-scale transient transfection and fluorescence-detection size-exclusion chromatography (FSEC) experiments using a GFP-His8-tagged candidate protein to screen for monodispersity and expression level. Once promising candidates are identified, we describe how to generate baculovirus, transduce HEK293S GnTI(-) (N-acetylglucosaminyltransferase I-negative) cells in suspension culture and overexpress the candidate protein. We have used these methods to prepare pure samples of chicken acid-sensing ion channel 1a (cASIC1) and Caenorhabditis elegans glutamate-gated chloride channel (GluCl) for X-ray crystallography, demonstrating how to rapidly and efficiently screen hundreds of constructs and accomplish large-scale expression in 4-6 weeks.
MeSH term(s)	Acid Sensing Ion Channels/genetics ; Acid Sensing Ion Channels/metabolism ; Animals ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Chickens ; Chloride Channels/genetics ; Chloride Channels/metabolism ; Chromatography, Gel ; Genetic Vectors ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; HEK293 Cells ; Histidine/genetics ; Humans ; Mammals ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; N-Acetylglucosaminyltransferases/metabolism ; Plasmids/genetics ; Protein Engineering/methods ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Transfection/methods
Chemical Substances	Acid Sensing Ion Channels ; Caenorhabditis elegans Proteins ; Chloride Channels ; Membrane Proteins ; Recombinant Proteins ; glutamate-gated chloride channels ; Green Fluorescent Proteins (147336-22-9) ; Histidine (4QD397987E) ; N-Acetylglucosaminyltransferases (EC 2.4.1.-) ; alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase I (EC 2.4.1.101)
Language	English
Publishing date	2014-10-09
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2244966-8
ISSN	1750-2799 ; 1754-2189
ISSN (online)	1750-2799
ISSN	1754-2189
DOI	10.1038/nprot.2014.173
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