The K/HDEL receptor does not recycle but instead acts as a Golgi-gatekeeper.
Autor: | Alvim JC; Centre for Plant Sciences, School of Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.; Laboratory of Plant Physiology and Biophysics, Bower Building, University of Glasgow, Glasgow, G12 8QQ, UK., Bolt RM; Centre for Plant Sciences, School of Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK., An J; Centre for Plant Sciences, School of Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK., Kamisugi Y; Centre for Plant Sciences, School of Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK., Cuming A; Centre for Plant Sciences, School of Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK., Silva-Alvim FAL; Centre for Plant Sciences, School of Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.; Laboratory of Plant Physiology and Biophysics, Bower Building, University of Glasgow, Glasgow, G12 8QQ, UK., Concha JO; Department of Cell and Molecular Biology, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, São Paulo, Brazil., daSilva LLP; Department of Cell and Molecular Biology, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, São Paulo, Brazil., Hu M; Centre for Plant Sciences, School of Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK., Hirsz D; Centre for Plant Sciences, School of Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK., Denecke J; Centre for Plant Sciences, School of Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK. j.denecke@leeds.ac.uk. |
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Jazyk: | angličtina |
Zdroj: | Nature communications [Nat Commun] 2023 Mar 23; Vol. 14 (1), pp. 1612. Date of Electronic Publication: 2023 Mar 23. |
DOI: | 10.1038/s41467-023-37056-0 |
Abstrakt: | Accurately measuring the ability of the K/HDEL receptor (ERD2) to retain the ER cargo Amy-HDEL has questioned earlier results on which the popular receptor recycling model is based upon. Here we demonstrate that ERD2 Golgi-retention, rather than fast ER export supports its function. Ligand-induced ERD2 redistribution is only observed when the C-terminus is masked or mutated, compromising the signal that prevents Golgi-to-ER transport of the receptor. Forcing COPI mediated retrograde transport destroys receptor function, but introducing ER-to-Golgi export or cis-Golgi retention signals re-activate ERD2 when its endogenous Golgi-retention signal is masked or deleted. We propose that ERD2 remains fixed as a Golgi gatekeeper, capturing K/HDEL proteins when they arrive and releasing them again into a subdomain for retrograde transport back to the ER. An in vivo ligand:receptor ratio far greater than 100 to 1 strongly supports this model, and the underlying mechanism appears to be extremely conserved across kingdoms. (© 2023. Crown.) |
Databáze: | MEDLINE |
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