AI Article Synopsis
- The ninaE-encoded Rh1 rhodopsin is crucial for the development and upkeep of the rhabdomere in Drosophila R1-6 photoreceptor cells, which is essential for light detection.
- Previous studies indicated that while bovine rhodopsin (Rho) can be expressed in Drosophila, it fails to maintain the rhabdomere structure after a week.
- Experiments using Rho-Rh1 chimeric rhodopsins identified that the cytoplasmic tail of Rh1 is key to ensuring the stability and organization of the rhabdomere.
Article Abstract
The ninaE-encoded Rh1 rhodopsin is the major light-sensitive pigment expressed in Drosophila R1-6 photoreceptor cells. Rh1 rhodopsin localizes to and is essential for the development and maintenance of the rhabdomere, the specialized membrane-rich organelle that serves as the site of phototransduction. We showed previously that the vertebrate bovine rhodopsin (Rho) is expressed and properly localized in Drosophila photoreceptor cells. Drosophila photoreceptors expressing only Rho have normal rhabdomere structure at young ages, but the rhabdomeres are not maintained and show extensive disorganization by 7-10 days of age. A series of Rho-Rh1 opsin chimeric rhodopsins were used to identify Rh1 domains required for maintenance of rhabdomeric structure. The results show that the Rh1 rhodopsin cytoplasmic tail domain, positioned to interact with cytoplasmic structural components, plays a major role in promoting rhabdomeric organization.
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