ArticleScientific reports2020
The KDEL trafficking receptor exploits pH to tune the strength of an unusual short hydrogen bond.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 21 citations in OpenAlex.
- Pyra-metho-carnil disrupts cancer cell proteostasis and induces apoptosis by binding to KDEL receptors.Scientific reports · 2026Article
- Computational Elucidation of Sterol Recognition by SREBP Cleavage Activatory Protein.Journal of chemical information and modeling · 2025Article
- Discovery of mono-ADP ribosylating toxins with high structural homology to Pseudomonas exotoxin A.Communications biology · 2025Article
- Endoplasmic reticulum homeostasis in plant-pathogen interactions: new scenarios for an old story.Journal of experimental botany · 2025Review
- Endoplasmic reticulum-targeted delivery of celastrol and PD-L1 siRNA for reinforcing immunogenic cell death and potentiating cancer immunotherapy.Acta pharmaceutica Sinica. B · 2024Article
- Molecular basis for pH sensing in the KDEL trafficking receptor.Structure (London, England : 1993) · 2024Article
- Intracellular cartilage oligomeric matrix protein augments breast cancer resistance to chemotherapy.Cell death & disease · 2024Article
- Does the KDEL receptor cycle between the Golgi and the ER?Nature communications · 2024Article
- Linear motifs regulating protein secretion, sorting and autophagy in Leishmania parasites are diverged with respect to their host equivalents.PLoS computational biology · 2024Article
- Mechanisms regulating the sorting of soluble lysosomal proteins.Bioscience reports · 2022Review
- KDEL Receptors: Pathophysiological Functions, Therapeutic Options, and Biotechnological Opportunities.Biomedicines · 2022Review
- Collagen transport and related pathways in Osteogenesis Imperfecta.Human genetics · 2021Review
- Article
- A virtuous cycle operated by ERp44 and ERGIC-53 guarantees proteostasis in the early secretory compartment.iScience · 2021Article
- Computational Modeling of C-Terminal Tails to Predict the Calcium-Dependent Secretion of Endoplasmic Reticulum Resident Proteins.Frontiers in chemistry · 2021Article
- Molecular basis for KDEL-mediated retrieval of escaped ER-resident proteins - SWEET talking the COPs.Journal of cell science · 2020Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The endoplasmic reticulum (ER) is the main site of protein synthesis in eukaryotic cells and requires a high concentration of luminal chaperones to function. During protein synthesis, ER luminal chaperones are swept along the secretory pathway and must be retrieved to maintain cell viability. ER protein retrieval is achieved by the KDEL receptor, which recognises a C-terminal Lys-Asp-Glu-Leu (KDEL) sequence. Recognition of ER proteins by the KDEL receptor is pH dependent, with binding occurring under acidic conditions in the Golgi and release under conditions of higher pH in the ER. Recent crystal structures of the KDEL receptor in the apo and peptide bound state suggested that peptide binding drives the formation of a short-hydrogen bond that locks the KDEL sequence in the receptor and activates the receptor for COPI binding in the cytoplasm. Using quantum mechanical calculations we demonstrate that the strength of this short hydrogen bond is reinforced following protonation of a nearby histidine, providing a conceptual link between receptor protonation and KDEL peptide binding. Protonation also controls the water networks adjacent to the peptide binding site, leading to a conformational change that ultimately allows the receptor-complex to be recognized by the COPI system.
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