Association of Shank 1A Scaffolding Protein with Cone Photoreceptor Terminals in the Mammalian Retina
Photoreceptor terminals contain post-synaptic density (PSD) proteins e.g., PSD-95/PSD-93, but their role at photoreceptor synapses is not known. PSDs are generally restricted to post-synaptic boutons in central neurons and form scaffolding with multiple proteins that have structural and functional r...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | en_US |
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Public Library of Science
2013
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| Online Access: | http://hdl.handle.net/1721.1/76645 |
| _version_ | 1811006237891887104 |
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| author | Salvatore, Stella, L., Jr. Vila, Alejandro Hung, Albert Y. Rome, Michael E. Huynh, Uyenchi Sheng, Morgan Hwa-Tze Kreienkamp, Hans-Jürgen Brecha, Nicholas C. |
| author2 | Picower Institute for Learning and Memory |
| author_facet | Picower Institute for Learning and Memory Salvatore, Stella, L., Jr. Vila, Alejandro Hung, Albert Y. Rome, Michael E. Huynh, Uyenchi Sheng, Morgan Hwa-Tze Kreienkamp, Hans-Jürgen Brecha, Nicholas C. |
| author_sort | Salvatore, Stella, L., Jr. |
| collection | MIT |
| description | Photoreceptor terminals contain post-synaptic density (PSD) proteins e.g., PSD-95/PSD-93, but their role at photoreceptor synapses is not known. PSDs are generally restricted to post-synaptic boutons in central neurons and form scaffolding with multiple proteins that have structural and functional roles in neuronal signaling. The Shank family of proteins (Shank 1–3) functions as putative anchoring proteins for PSDs and is involved in the organization of cytoskeletal/signaling complexes in neurons. Specifically, Shank 1 is restricted to neurons and interacts with both receptors and signaling molecules at central neurons to regulate plasticity. However, it is not known whether Shank 1 is expressed at photoreceptor terminals. In this study we have investigated Shank 1A localization in the outer retina at photoreceptor terminals. We find that Shank 1A is expressed presynaptically in cone pedicles, but not rod spherules, and it is absent from mice in which the Shank 1 gene is deleted. Shank 1A co-localizes with PSD-95, peanut agglutinin, a marker of cone terminals, and glycogen phosphorylase, a cone specific marker. These findings provide convincing evidence for Shank 1A expression in both the inner and outer plexiform layers, and indicate a potential role for PSD-95/Shank 1 complexes at cone synapses in the outer retina. |
| first_indexed | 2024-09-23T16:48:55Z |
| format | Article |
| id | mit-1721.1/76645 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T16:48:55Z |
| publishDate | 2013 |
| publisher | Public Library of Science |
| record_format | dspace |
| spelling | mit-1721.1/766452022-10-03T08:28:13Z Association of Shank 1A Scaffolding Protein with Cone Photoreceptor Terminals in the Mammalian Retina Salvatore, Stella, L., Jr. Vila, Alejandro Hung, Albert Y. Rome, Michael E. Huynh, Uyenchi Sheng, Morgan Hwa-Tze Kreienkamp, Hans-Jürgen Brecha, Nicholas C. Picower Institute for Learning and Memory Hung, Albert Y. Sheng, Morgan Hwa-Tze Photoreceptor terminals contain post-synaptic density (PSD) proteins e.g., PSD-95/PSD-93, but their role at photoreceptor synapses is not known. PSDs are generally restricted to post-synaptic boutons in central neurons and form scaffolding with multiple proteins that have structural and functional roles in neuronal signaling. The Shank family of proteins (Shank 1–3) functions as putative anchoring proteins for PSDs and is involved in the organization of cytoskeletal/signaling complexes in neurons. Specifically, Shank 1 is restricted to neurons and interacts with both receptors and signaling molecules at central neurons to regulate plasticity. However, it is not known whether Shank 1 is expressed at photoreceptor terminals. In this study we have investigated Shank 1A localization in the outer retina at photoreceptor terminals. We find that Shank 1A is expressed presynaptically in cone pedicles, but not rod spherules, and it is absent from mice in which the Shank 1 gene is deleted. Shank 1A co-localizes with PSD-95, peanut agglutinin, a marker of cone terminals, and glycogen phosphorylase, a cone specific marker. These findings provide convincing evidence for Shank 1A expression in both the inner and outer plexiform layers, and indicate a potential role for PSD-95/Shank 1 complexes at cone synapses in the outer retina. National Institutes of Health (U.S.) (K08 Award NS41411) Howard Hughes Medical Institute (Investigator) 2013-01-30T15:17:09Z 2013-01-30T15:17:09Z 2012-09 2012-04 Article http://purl.org/eprint/type/JournalArticle 1932-6203 http://hdl.handle.net/1721.1/76645 Stella, Salvatore L. et al. “Association of Shank 1A Scaffolding Protein with Cone Photoreceptor Terminals in the Mammalian Retina.” Ed. Karl-Wilhelm Koch. PLoS ONE 7.9 (2012): e43463. en_US http://dx.doi.org/10.1371/journal.pone.0043463 PLoS ONE Creative Commons Attribution http://creativecommons.org/licenses/by/2.5/ application/pdf Public Library of Science PLoS |
| spellingShingle | Salvatore, Stella, L., Jr. Vila, Alejandro Hung, Albert Y. Rome, Michael E. Huynh, Uyenchi Sheng, Morgan Hwa-Tze Kreienkamp, Hans-Jürgen Brecha, Nicholas C. Association of Shank 1A Scaffolding Protein with Cone Photoreceptor Terminals in the Mammalian Retina |
| title | Association of Shank 1A Scaffolding Protein with Cone Photoreceptor Terminals in the Mammalian Retina |
| title_full | Association of Shank 1A Scaffolding Protein with Cone Photoreceptor Terminals in the Mammalian Retina |
| title_fullStr | Association of Shank 1A Scaffolding Protein with Cone Photoreceptor Terminals in the Mammalian Retina |
| title_full_unstemmed | Association of Shank 1A Scaffolding Protein with Cone Photoreceptor Terminals in the Mammalian Retina |
| title_short | Association of Shank 1A Scaffolding Protein with Cone Photoreceptor Terminals in the Mammalian Retina |
| title_sort | association of shank 1a scaffolding protein with cone photoreceptor terminals in the mammalian retina |
| url | http://hdl.handle.net/1721.1/76645 |
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