@article{2cf509998aa24aca8e9dad5693ebf225,
title = "Xport-A functions as a chaperone by stabilizing the first five transmembrane domains of rhodopsin-1",
abstract = "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.",
keywords = "Biochemistry, Biological sciences, Molecular biology, Molecular interaction",
author = "Gaspar, {Catarina J.} and Tiago Gomes and Martins, {Joana C.} and Melo, {Manuel N.} and Colin Adrain and Cordeiro, {Tiago N.} and Domingos, {Pedro M.}",
note = "Funding Information: The authors acknowledge Funda{\c c}{\~a}o para a Ci{\^e}ncia e a Tecnologia, I.P. (FCT) for funding project MOSTMICRO-ITQB , with references UIDB/04612/2020 and UIDP/04612/2020 . M.N.M. further acknowledges FCT for fellowship CEECIND/04124/2017 and T.N.C. is the recipient of the grant CEECIND/01443/2017 . The project leading to these results was funded by the grants LCF/PR/HR17/52150018 ( 'la Caixa' Foundation ), FCT AGA-KHAN/541141368/2019 ( FCT and Aga Khan Foundation ), and SR&TD project ( PTDC/BIA-BFS/0391/2021 ). Publisher Copyright: {\textcopyright} 2023 The Authors",
year = "2023",
month = dec,
day = "15",
doi = "10.1016/j.isci.2023.108309",
language = "English",
volume = "26",
journal = "ISCIENCE",
issn = "2589-0042",
publisher = "Elsevier",
number = "12",
}