RIBEYE, a Component of Synaptic Ribbons
Open accessAbstract
Photoreceptor cells utilize ribbon synapses to transmit sensory signals at high resolution. Ribbon synapses release neurotransmitters tonically, with a high release rate made possible by continuous docking of synaptic vesicles on presynaptic ribbons. We have partially purified synaptic ribbons from retina and identified a major protein component called RIBEYE. RIBEYE is composed of a unique A domain specific for ribbons, and a B domain identical with CtBP2, a transcriptional repressor that in turn is related to 2-hydroxyacid dehydrogenases. The A domain mediates assembly of RIBEYE into large structures, whereas the B domain binds NAD(+) with high affinity, similar to 2-hydroxyacid dehydrogenases. Our results define a unique component of synaptic ribbons and suggest that RIBEYE evolved in vertebrates under utilization of a preexisting protein to build a unique scaffold for a specialized synapse.
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Synaptic ribbons probably arose in vertebrates with the generation of RIBEYE.
“Evolutionarily, synaptic ribbons probably arose in vertebrates with the generation of RIBEYE, their major protein component that represents a fusion of a novel N-terminal domain encoded by a single large exon with another protein called CtBP2 (Schmitz et al., 2000).”
From The Presynaptic Active Zone (2012) · cites this paper as Schmitz et al., 2000
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- Authors
- Schmitz, F., Königstorfer, A., & Südhof, T. C.
- Affiliations
- Howard Hughes Medical Institute (US)
- Max Planck Institute of Experimental Medicine (DE)
- Corresponding author
- Südhof, Thomas C.
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2000-12
- Volume
- 28
- Issue
- 3
- Pages
- 857-872
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2005019117
- Cited by
- 581
- References
- 0
- Citations by year
- 2026: 18 · 2025: 21 · 2024: 34 · 2023: 20 · 2022: 22 · 2021: 22 · 2020: 26 · 2019: 27 · 2018: 22 · 2017: 25 · 2016: 30 · 2015: 29 · 2014: 32 · 2013: 29 · 2012: 31
- FWCI
- 2.98
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinal Development and Disorders
- Keywords
- ribeye, synaptic ribbons, ribbon synapses, photoreceptors, synaptic vesicle docking, neurotransmitter release, CtBP2, transcriptional repressor, NAD+ binding, protein domain evolution
- MeSH terms
- Alcohol Oxidoreductases, Animals, Cattle, Cells, Cultured, DNA-Binding Proteins, Eye Proteins, Fibroblasts, Humans, Molecular Sequence Data, NAD, Nerve Tissue Proteins, Organ Specificity, Phosphoproteins, Repressor Proteins, Retina, Structure-Activity Relationship, Synaptic Membranes, Transfection, Organelles, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Evolution, Molecular, Rats, Co-Repressor Proteins
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