ArticleThe EMBO journal2001
Recruitment to Golgi membranes of ADP-ribosylation factor 1 is mediated by the cytoplasmic domain of p23.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 117 citations in OpenAlex.
- The ER-Golgi intermediate compartment: a central hub integrating membrane trafficking and stress responses.EMBO reports · 2026Review
- The Activation of ARF1 Is Dynamically Regulated by its Palmitoylation.Molecular & cellular proteomics : MCP · 2026Article
- ARF GTPases Function at the Golgi.Sub-cellular biochemistry · 2026Review
- p24-Tango1 interactions ensure ER-Golgi interface stability and efficient transport.The Journal of cell biology · 2024Article
- STED imaging of endogenously tagged ARF GTPases reveals their distinct nanoscale localizations.The Journal of cell biology · 2023Article
- Transmembrane p24 trafficking protein 10 (TMED10) inhibits mitochondrial damage and protects neurons in ischemic stroke via the c-Jun N-terminal kinase (JNK) signaling pathway.Experimental animals · 2023Article
- Kinetics of Arf1 inactivation regulates Golgi organisation and function in non-adherent fibroblasts.Biology open · 2023Article
- A Novel Protein Encoded by Exosomal CircATG4B Induces Oxaliplatin Resistance in Colorectal Cancer by Promoting Autophagy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
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- ACBD3 modulates KDEL receptor interaction with PKA for its trafficking via tubulovesicular carrier.BMC biology · 2021Article
- p53 loss activates prometastatic secretory vesicle biogenesis in the Golgi.Science advances · 2021Article
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- TMP21 in Alzheimer's Disease: Molecular Mechanisms and a Potential Target.Frontiers in cellular neuroscience · 2019Review
- The Arf-GDP-regulated recruitment of GBF1 to Golgi membranes requires domains HDS1 and HDS2 and a Golgi-localized protein receptor.Journal of cell science · 2018Article
- A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi.Molecular biology of the cell · 2017Article
- Protein sorting at the ER-Golgi interface.The Journal of cell biology · 2016Review
- GTP-binding of ARL-3 is activated by ARL-13 as a GEF and stabilized by UNC-119.Scientific reports · 2016Article
- Trafficking of glycosylphosphatidylinositol anchored proteins from the endoplasmic reticulum to the cell surface.Journal of lipid research · 2016Review
- The Identification of Novel Protein-Protein Interactions in Liver that Affect Glucagon Receptor Activity.PloS one · 2015Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Binding to Golgi membranes of ADP ribosylation factor 1 (ARF1) is the first event in the initiation of COPI coat assembly. Based on binding studies, a proteinaceous receptor has been proposed to be critical for this process. We now report that p23, a member of the p24 family of Golgi-resident transmembrane proteins, is involved in ARF1 binding to membranes. Using a cross-link approach based on a photolabile peptide corresponding to the cytoplasmic domain of p23, the GDP form of ARF1 (ARF1-GDP) is shown to interact with p23 whereas ARF1-GTP has no detectable affinity to p23. The p23 binding is shown to localize specifically to a 22 amino acid C-terminal fragment of ARF1. While a monomeric form of a non-photolabile p23 peptide does not significantly inhibit formation of the cross-link product, the corresponding dimeric form does compete efficiently for this interaction. Consistently, the dimeric p23 peptide strongly inhibits ARF1 binding to native Golgi membranes suggesting that an oligomeric form of p23 acts as a receptor for ARF1 before nucleotide exchange takes place.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.