Xport-A functions as a chaperone by stabilizing the first five transmembrane domains of rhodopsin-1
Summary: Rhodopsin-1 (Rh1), the main photosensitive protein of Drosophila, is a seven-transmembrane domain protein, which is inserted co-translationally in the endoplasmic reticulum (ER) membrane. Biogenesis of Rh1 occurs in the ER, where various chaperones interact with Rh1 to aid in its folding an...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2023-12-01
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| Series: | iScience |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2589004223023866 |
| _version_ | 1827582097235116032 |
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| author | Catarina J. Gaspar Tiago Gomes Joana C. Martins Manuel N. Melo Colin Adrain Tiago N. Cordeiro Pedro M. Domingos |
| author_facet | Catarina J. Gaspar Tiago Gomes Joana C. Martins Manuel N. Melo Colin Adrain Tiago N. Cordeiro Pedro M. Domingos |
| author_sort | Catarina J. Gaspar |
| collection | DOAJ |
| description | Summary: Rhodopsin-1 (Rh1), the main photosensitive protein of Drosophila, is a seven-transmembrane domain protein, which is inserted co-translationally in the endoplasmic reticulum (ER) membrane. Biogenesis of Rh1 occurs in the ER, where various chaperones interact with Rh1 to aid in its folding and subsequent transport from the ER to the rhabdomere, the light-sensing organelle of the photoreceptors. Xport-A has been proposed as a chaperone/transport factor for Rh1, but the exact molecular mechanism for Xport-A activity upon Rh1 is unknown. Here, we propose a model where Xport-A functions as a chaperone during the biogenesis of Rh1 in the ER by stabilizing the first five transmembrane domains (TMDs) of Rh1. |
| first_indexed | 2024-03-08T22:45:39Z |
| format | Article |
| id | doaj.art-d33cb3e63f994da2941e4244b8c4b3b1 |
| institution | Directory Open Access Journal |
| issn | 2589-0042 |
| language | English |
| last_indexed | 2024-03-08T22:45:39Z |
| publishDate | 2023-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | iScience |
| spelling | doaj.art-d33cb3e63f994da2941e4244b8c4b3b12023-12-17T06:40:24ZengElsevieriScience2589-00422023-12-012612108309Xport-A functions as a chaperone by stabilizing the first five transmembrane domains of rhodopsin-1Catarina J. Gaspar0Tiago Gomes1Joana C. Martins2Manuel N. Melo3Colin Adrain4Tiago N. Cordeiro5Pedro M. Domingos6Instituto de Tecnologia Química e Biológica da Universidade Nova de Lisboa (ITQB-NOVA), Av. da República, 2780-157 Oeiras, Portugal; Membrane Traffic Lab, Instituto Gulbenkian de Ciência (IGC), 2780-156 Oeiras, PortugalInstituto de Tecnologia Química e Biológica da Universidade Nova de Lisboa (ITQB-NOVA), Av. da República, 2780-157 Oeiras, PortugalInstituto de Tecnologia Química e Biológica da Universidade Nova de Lisboa (ITQB-NOVA), Av. da República, 2780-157 Oeiras, PortugalInstituto de Tecnologia Química e Biológica da Universidade Nova de Lisboa (ITQB-NOVA), Av. da República, 2780-157 Oeiras, PortugalMembrane Traffic Lab, Instituto Gulbenkian de Ciência (IGC), 2780-156 Oeiras, Portugal; Patrick G Johnston Centre for Cancer Research, Queen’s University Belfast, 97 Lisburn Road, BT9 7AE Belfast, UK; Corresponding authorInstituto de Tecnologia Química e Biológica da Universidade Nova de Lisboa (ITQB-NOVA), Av. da República, 2780-157 Oeiras, Portugal; Corresponding authorInstituto de Tecnologia Química e Biológica da Universidade Nova de Lisboa (ITQB-NOVA), Av. da República, 2780-157 Oeiras, Portugal; Corresponding authorSummary: Rhodopsin-1 (Rh1), the main photosensitive protein of Drosophila, is a seven-transmembrane domain protein, which is inserted co-translationally in the endoplasmic reticulum (ER) membrane. Biogenesis of Rh1 occurs in the ER, where various chaperones interact with Rh1 to aid in its folding and subsequent transport from the ER to the rhabdomere, the light-sensing organelle of the photoreceptors. Xport-A has been proposed as a chaperone/transport factor for Rh1, but the exact molecular mechanism for Xport-A activity upon Rh1 is unknown. Here, we propose a model where Xport-A functions as a chaperone during the biogenesis of Rh1 in the ER by stabilizing the first five transmembrane domains (TMDs) of Rh1.http://www.sciencedirect.com/science/article/pii/S2589004223023866BiochemistryBiological sciencesMolecular biologyMolecular interaction |
| spellingShingle | Catarina J. Gaspar Tiago Gomes Joana C. Martins Manuel N. Melo Colin Adrain Tiago N. Cordeiro Pedro M. Domingos Xport-A functions as a chaperone by stabilizing the first five transmembrane domains of rhodopsin-1 iScience Biochemistry Biological sciences Molecular biology Molecular interaction |
| title | Xport-A functions as a chaperone by stabilizing the first five transmembrane domains of rhodopsin-1 |
| title_full | Xport-A functions as a chaperone by stabilizing the first five transmembrane domains of rhodopsin-1 |
| title_fullStr | Xport-A functions as a chaperone by stabilizing the first five transmembrane domains of rhodopsin-1 |
| title_full_unstemmed | Xport-A functions as a chaperone by stabilizing the first five transmembrane domains of rhodopsin-1 |
| title_short | Xport-A functions as a chaperone by stabilizing the first five transmembrane domains of rhodopsin-1 |
| title_sort | xport a functions as a chaperone by stabilizing the first five transmembrane domains of rhodopsin 1 |
| topic | Biochemistry Biological sciences Molecular biology Molecular interaction |
| url | http://www.sciencedirect.com/science/article/pii/S2589004223023866 |
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