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bioRxiv · 10.1101/2022.04.01.486763

Xport-A functions as a chaperone by stabilizing the first 5 transmembrane domains of Rhodopsin-1

Gaspar, C. J.·Martins, J. C.·Melo, M. N.·Cordeiro, T. N.·Adrain, C.·Domingos, P. M.
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Abstract

Rhodopsin-1 (Rh1), the main photo-sensitive protein of Drosophila, is a seven transmembrane domain protein, which is inserted co-translationally in the endoplasmic reticulum (ER) membrane. Maturation of Rh1 occurs in the ER, where various chaperones interact with Rh1 to aid in its folding and subsequent transport in the secretory pathway. Xport-A has been shown to be a chaperone/ transport factor for Rh1, but the exact molecular mechanism for Xport-A activity upon Rh1 is not known. Here, based on computational predictions, we propose a model where Xport-A functions as a chaperone in the biosynthesis of Rh1 by stabilizing the first 5 transmembrane domains of Rh1, but not the full length Rh1 protein.

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Gaspar, C. J., Martins, J. C., Melo, M. N., Cordeiro, T. N., Adrain, C., Domingos, P. M.. 2022-04-02. Xport-A functions as a chaperone by stabilizing the first 5 transmembrane domains of Rhodopsin-1. https://doi.org/10.1101/2022.04.01.486763

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