ArticleNature communications2023
The K/HDEL receptor does not recycle but instead acts as a Golgi-gatekeeper.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- Atypical endo-β-1,4-mannanases are necessary for normal glucomannan synthesis in Arabidopsis.Plant physiology · 2026Article
- A regulatory circuit operated by KDELR1 and KDELR3 fine-tunes the composition of the early secretory pathway.Cellular and molecular life sciences : CMLS · 2026Article
- Signalling pathways and cellular functions of KDEL receptors: implications in cancer biology.Cellular and molecular life sciences : CMLS · 2025Review
- Decoding PDI diversity: Insights into structure, domains, and functionality in sorghum.Computational and structural biotechnology journal · 2025Article
- Trafficking and localization of Golgi-residentFrontiers in plant science · 2025Review
- An RXLR effector disrupts vesicle trafficking at ER-Golgi interface for Phytophthora capsici pathogenicity.Molecules and cells · 2024Article
- Exploring the potential biological significance of KDELR family genes in lung adenocarcinoma.Scientific reports · 2024Article
- Does the KDEL receptor cycle between the Golgi and the ER?Nature communications · 2024Article
- Reply to: Does the KDEL receptor cycle between the Golgi and the ER?Nature communications · 2024Article
- Spatiotemporal dissection of the Golgi apparatus and the ER-Golgi intermediate compartment in budding yeast.eLife · 2024Article
- Studying Secretory Protein Synthesis in Nicotiana benthamiana Protoplasts.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Phytaspase Is Capable of Detaching the Endoplasmic Reticulum Retrieval Signal from Tobacco Calreticulin-3.International journal of molecular sciences · 2023Article
- Disease-Associated Factors at the Endoplasmic Reticulum-Golgi Interface.Traffic (Copenhagen, Denmark)Review
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
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.
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