KDELR2

Last update 08 May 2025

Basic Info

Synonyms

ELP-1, ER lumen protein-retaining receptor 2, ERD2-like protein 1

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Introduction

Membrane receptor that binds the K-D-E-L sequence motif in the C-terminal part of endoplasmic reticulum resident proteins and maintains their localization in that compartment by participating to their vesicle-mediated recycling back from the Golgi (PubMed:1325562, PubMed:18086916, PubMed:33053334). Binding is pH dependent, and is optimal at pH 5-5.4 (By similarity).

100 Clinical Results associated with KDELR2

100 Translational Medicine associated with KDELR2

0 Patents (Medical) associated with KDELR2

152

Literatures (Medical) associated with KDELR2

01 Mar 2025·Carbohydrate Polymers

The efficient separation of bioactive components from Eucommia ulmoides Oliver using membrane filtration technology and its mechanisms in preventing alcoholic liver disease

Article

Author: Zhu, Ming-Qiang ; Chi, Zhi-Zheng ; Qing, Ren-Yan ; Gao, Ming-Qing ; Long, Da-Ping ; Yin, Shuang-Shuang ; Le, Xiao-Na

The efficient extraction and purification of active components from Eucommia ulmoides Oliver (EUO) are crucial for their utilization. The structure and properties of the prepared EUO leaf polysaccharides (ELPs) and extractum (ELE) were comprehensively characterized in this study, and the intervention mechanism of the EUO polysaccharides and extractum in alcoholic liver disease (ALD) were investigated. The yield of EUO extractum was 24.82 %, from which nine active components were identified. The yield of EUO leaf polysaccharides was 8.06 %, and the polysaccharides were fractionated into three components ELP1, ELP2, and ELP3 through ultrafiltration technology, with yields of 4.19 %, 1.26 %, and 2.59 %, respectively. Ultrafiltration significantly reduced protein content, enhanced polysaccharide homogeneity, and altered monosaccharide composition. ELP3 exhibited higher scavenging efficacy on •OH and ABTS•⁺ than ELP1 and ELP2, reaching 82.53 % and 88.41 % respectively. ELP3 and ELE intervention preserved liver integrity, mitigated lipid accumulation and inflammation, and regulated hepatic oxidative stress. Moreover, they maintained intestinal barrier function, suppressed harmful bacteria (Escherichia-Shigella, and UBA1819), and promoted beneficial bacteria (Dubosiella, Monoglobus, and Lachnospiraceae). Thirteen hallmark differential metabolites were identified, and KEGG pathway enrichment analysis suggested that ELP3 and ELE may ameliorate ALD through pathways like longevity regulation, choline metabolism in cancer, oxidative phosphorylation, and AMPK signaling pathway. This investigation holds significance in delineating the beneficial effects of ELP3 and ELE in ALD alleviation.

01 Mar 2025·Journal of Biological Chemistry

Topology-driven discovery of transmembrane protein S-palmitoylation

Article

Author: Forrester, Michael T ; Waddell, Farrah D ; Singh, Rohit ; Egol, Jacob R ; Ozbay, Sinan ; Tata, Purushothama Rao

Protein S-palmitoylation is a reversible lipophilic posttranslational modification regulating diverse signaling pathways. Within transmembrane proteins (TMPs), S-palmitoylation is implicated in conditions from inflammatory disorders to respiratory viral infections. Many small-scale experiments have observed S-palmitoylation at juxtamembrane Cys residues. However, most large-scale S-palmitoyl discovery efforts rely on trypsin-based proteomics within which hydrophobic juxtamembrane regions are likely underrepresented. Machine learning-by virtue of its freedom from experimental constraints-is particularly well suited to address this discovery gap surrounding TMP S-palmitoylation. Utilizing a UniProt-derived feature set, a gradient-boosted machine learning tool (TopoPalmTree) was constructed and applied to a holdout dataset of viral S-palmitoylated proteins. Upon application to the mouse TMP proteome, 1591 putative S-palmitoyl sites (i.e. not listed in SwissPalm or UniProt) were identified. Two lung-expressed S-palmitoyl candidates (synaptobrevin Vamp5 and water channel Aquaporin-5) were experimentally assessed, as were three Type I transmembrane proteins (Cadm4, Chodl, and Havcr2). Finally, TopoPalmTree was used for the rational design of an S-palmitoyl site on KDEL-Receptor 2. This readily interpretable model aligns the innumerable small-scale experiments observing juxtamembrane S-palmitoylation into a proteomic tool for TMP S-palmitoyl discovery and design, thus facilitating future investigations of this important modification.

01 Feb 2025·European Journal of Medicinal Chemistry

Correction of aberrant splicing of ELP1 pre-mRNA by kinetin derivatives – A structure activity relationship study

Article

Author: Maková, Barbara ; Doležal, Karel ; Medvedíková, Martina ; Zatloukal, Marek ; Hönig, Martin ; Hajdúch, Marián ; Hořínková, Alena ; Voller, Jiří ; Oždian, Tomáš ; Mik, Václav ; Vojta, Petr ; Strnad, Miroslav ; Forejt, Kristýna ; Drašarová, Lenka ; Plíhalová, Lucie ; Lišková, Barbora

Familial dysautonomia is a debilitating congenital neurodegenerative disorder with no causative therapy. It is caused by a homozygous mutation in ELP1 gene, resulting in the production of the transcript lacking exon 20. The compounds studied as potential treatments include the clinical candidate kinetin, a plant hormone from the cytokinin family. We explored the relationship between the structure of a set of kinetin derivatives (N = 72) and their ability to correct aberrant splicing of the ELP1 gene. Active compounds can be obtained by the substitution of the purine ring with chlorine and fluorine at the C2 atom, with a small alkyl group at the N7 atom, or with diverse groups at the C8 atom. On the other hand, a substitution at the N3 or N9 atoms resulted in a loss of activity. We successfully tested a hypothesis inspired by the remarkable tolerance of the position C8 to substitution, postulating that the imidazole of the purine moiety is not required for the activity. We also evaluated the activity of phytohormones from other families, but none of them corrected ELP1 mRNA aberrant splicing. A panel of in vitro ADME assays, including evaluation of transport across model barriers, stability in plasma and in the presence of liver microsomal fraction as well as plasma protein binding, was used for an initial estimation of the potential bioavailability of the active compounds. Finally, a RNA-seq data suggest that 8-aminokinetin modulates expression spliceosome components.

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KDELR2

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