Xport-A functions as a chaperone by stabilizing the first five transmembrane domains of rhodopsin-1
Year: 2023
Type: article
Abstract: , 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.
Source: iScience
Language: English
Topic: Heat shock proteins research
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $3,150
Awards: G1104823683, G1254282178, Arquitectura de uma plataforma de sinalização patogénica, G3029852638, G310293013, G3739215670, G5454278309, G5949521807, G6119538036, Microbiologia Molecular, Estrutural e Celular - – Instituto de Tecnologia Química e Biológica António Xavier, Microbiologia Molecular, Estrutural e Celular - – Instituto de Tecnologia Química e Biológica António Xavier
OpenAlex ID: W4387873284