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Xport-A functions as a chaperone by stabilizing the first 5 transmembrane domains of Rhodopsin-1
Open accessPreprint — published as 10.1016/j.isci.2023.108309
Abstract
Summary: 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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Metadata
- Authors
- Gaspar, C. J., Martins, J. C., Melo, M. N., Cordeiro, T. N., Adrain, C., & Domingos, P. M.
- Affiliations
- Instituto de Tecnologia Química e Biológica António Xavier (PT)
- Queen's University Belfast (GB)
- Corresponding author
- Cordeiro, Tiago N
- Adrain, Colin
- Domingos, Pedro M
- Venue
- iScience
- Publisher
- openRxiv
- Published
- 2022-04-02
- Volume
- 26
- Issue
- 12
- Pages
- 108309-108309
- ISSN
- 2589-0042 (ISSN-L)
- PMC
- PMC10663829
- OpenAlex
- W4387873284
- Cited by
- 2
- References
- 1
- Citations by year
- 2026: 1 · 2025: 1
- FWCI
- 0.18
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- iScience (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Research Portal (Queen's University Belfast) (publishedVersion, cc-by-nc-nd)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, other-oa)
- Funders
- Aga Khan Foundation (FCT AGA-KHAN/541141368/2019)
- “la Caixa” Foundation (AGA-KHAN/541141368/2019)
- Fundación Bancaria Caixa d'Estalvis i Pensions de Barcelona
- Fundação para a Ciência e a Tecnologia (CEECIND/01443/2017, PTDC/BIA-BFS/0391/2021, UIDB/04612/2020 and UIDP/04612/2020, CEECIND/04124/2017, LCF/PR/HR17/52150018, /2017, FCT AGA-KHAN/541141368/2019, UIDP/04612/2020, UIDB/04612/2020)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Keywords
- chaperone activity, seven-transmembrane proteins, endoplasmic reticulum membrane insertion, co-translational insertion, protein folding
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