| First Author | Schmitz F | Year | 2000 |
| Journal | Neuron | Volume | 28 |
| Issue | 3 | Pages | 857-72 |
| PubMed ID | 11163272 | Mgi Jnum | J:66510 |
| Mgi Id | MGI:1928571 | Doi | 10.1016/s0896-6273(00)00159-8 |
| Citation | Schmitz F, et al. (2000) RIBEYE, a component of synaptic ribbons: a protein's journey through evolution provides insight into synaptic ribbon function. Neuron 28(3):857-72 |
| abstractText | 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. |
