Cell
Volume 67, Issue 2, 18 October 1991, Pages 255-263
Journal home page for Cell

The cyclophilin homolog ninaA is required in the secretory pathway

https://doi.org/10.1016/0092-8674(91)90177-ZGet rights and content

Summary

In Drosophila, the major rhodopsin Rh1 is synthesized in endoplasmic reticuIum (ER)-bound ribosomes of the R1-R6 photoreceptor cells and is then transported to the rhabdomeres where it functions in phototransduction. Mutations in the cyclophilin homolog ninaA lead to a 90% reduction in Rhl opsin. Cyclophilins have been shown to be peptidyl-prolyl cis-trans isomerases and have been implicated in catalyzing protein folding. We now show that mutations in the ninaA gene severely inhibit opsin transport from the ER, leading to dramatic accumulations of ER cisternae in the photoreceptor cells. These results demonstrate that ninaA functions in the ER. Interestingly, ninaA and Rh1 also colocalize to secretory vesicles, suggesting that Rh1 may require ninaA as it travels through the distal compartments of the secretory pathway. These results are discussed in relation to the possible role of cyclophilins in protein folding and intracellular protein traflicking.

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