Photoreceptor Compartment-Specific TULP1 Interactomes
Photoreceptors are highly compartmentalized cells with large amounts of proteins synthesized in the inner segment (IS) and transported to the outer segment (OS) and synaptic terminal. Tulp1 is a photoreceptor-specific protein localized to the IS and synapse. In the absence of Tulp1, several OS-speci...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-07-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/22/15/8066 |
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| author | Lindsey A. Ebke Satyabrata Sinha Gayle J. T. Pauer Stephanie A. Hagstrom |
| author_facet | Lindsey A. Ebke Satyabrata Sinha Gayle J. T. Pauer Stephanie A. Hagstrom |
| author_sort | Lindsey A. Ebke |
| collection | DOAJ |
| description | Photoreceptors are highly compartmentalized cells with large amounts of proteins synthesized in the inner segment (IS) and transported to the outer segment (OS) and synaptic terminal. Tulp1 is a photoreceptor-specific protein localized to the IS and synapse. In the absence of Tulp1, several OS-specific proteins are mislocalized and synaptic vesicle recycling is impaired. To better understand the involvement of Tulp1 in protein trafficking, our approach in the current study was to physically isolate Tulp1-containing photoreceptor compartments by serial tangential sectioning of retinas and to identify compartment-specific Tulp1 binding partners by immunoprecipitation followed by liquid chromatography tandem mass spectrometry. Our results indicate that Tulp1 has two distinct interactomes. We report the identification of: (1) an IS-specific interaction between Tulp1 and the motor protein Kinesin family member 3a (Kif3a), (2) a synaptic-specific interaction between Tulp1 and the scaffold protein Ribeye, and (3) an interaction between Tulp1 and the cytoskeletal protein microtubule-associated protein 1B (MAP1B) in both compartments. Immunolocalization studies in the wild-type retina indicate that Tulp1 and its binding partners co-localize to their respective compartments. Our observations are compatible with Tulp1 functioning in protein trafficking in multiple photoreceptor compartments, likely as an adapter molecule linking vesicles to molecular motors and the cytoskeletal scaffold. |
| first_indexed | 2024-03-10T09:15:07Z |
| format | Article |
| id | doaj.art-9270affc87ff45c9baafec887d1979cd |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T09:15:07Z |
| publishDate | 2021-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-9270affc87ff45c9baafec887d1979cd2023-11-22T05:42:41ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-07-012215806610.3390/ijms22158066Photoreceptor Compartment-Specific TULP1 InteractomesLindsey A. Ebke0Satyabrata Sinha1Gayle J. T. Pauer2Stephanie A. Hagstrom3Department of Ophthalmic Research, Cole Eye Institute, Cleveland Clinic, Cleveland, OH 44195, USADepartment of Ophthalmic Research, Cole Eye Institute, Cleveland Clinic, Cleveland, OH 44195, USADepartment of Ophthalmic Research, Cole Eye Institute, Cleveland Clinic, Cleveland, OH 44195, USADepartment of Ophthalmic Research, Cole Eye Institute, Cleveland Clinic, Cleveland, OH 44195, USAPhotoreceptors are highly compartmentalized cells with large amounts of proteins synthesized in the inner segment (IS) and transported to the outer segment (OS) and synaptic terminal. Tulp1 is a photoreceptor-specific protein localized to the IS and synapse. In the absence of Tulp1, several OS-specific proteins are mislocalized and synaptic vesicle recycling is impaired. To better understand the involvement of Tulp1 in protein trafficking, our approach in the current study was to physically isolate Tulp1-containing photoreceptor compartments by serial tangential sectioning of retinas and to identify compartment-specific Tulp1 binding partners by immunoprecipitation followed by liquid chromatography tandem mass spectrometry. Our results indicate that Tulp1 has two distinct interactomes. We report the identification of: (1) an IS-specific interaction between Tulp1 and the motor protein Kinesin family member 3a (Kif3a), (2) a synaptic-specific interaction between Tulp1 and the scaffold protein Ribeye, and (3) an interaction between Tulp1 and the cytoskeletal protein microtubule-associated protein 1B (MAP1B) in both compartments. Immunolocalization studies in the wild-type retina indicate that Tulp1 and its binding partners co-localize to their respective compartments. Our observations are compatible with Tulp1 functioning in protein trafficking in multiple photoreceptor compartments, likely as an adapter molecule linking vesicles to molecular motors and the cytoskeletal scaffold.https://www.mdpi.com/1422-0067/22/15/8066Tulp1photoreceptor degenerationsynapseciliaprotein traffickingproteomics |
| spellingShingle | Lindsey A. Ebke Satyabrata Sinha Gayle J. T. Pauer Stephanie A. Hagstrom Photoreceptor Compartment-Specific TULP1 Interactomes International Journal of Molecular Sciences Tulp1 photoreceptor degeneration synapse cilia protein trafficking proteomics |
| title | Photoreceptor Compartment-Specific TULP1 Interactomes |
| title_full | Photoreceptor Compartment-Specific TULP1 Interactomes |
| title_fullStr | Photoreceptor Compartment-Specific TULP1 Interactomes |
| title_full_unstemmed | Photoreceptor Compartment-Specific TULP1 Interactomes |
| title_short | Photoreceptor Compartment-Specific TULP1 Interactomes |
| title_sort | photoreceptor compartment specific tulp1 interactomes |
| topic | Tulp1 photoreceptor degeneration synapse cilia protein trafficking proteomics |
| url | https://www.mdpi.com/1422-0067/22/15/8066 |
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