Recruitment to Golgi membranes of ADP-ribosylation factor 1 is mediated by the cytoplasmic domain of p23
Autor: | Friedrich Lottspeich, Felix T. Wieland, Daniel U. Gommel, Abdul Razaque Memon, Walter Nickel, Constanze Reinhard, Jens Pfannstiel, J. Bernd Helms, Johannes Lechner, Armin Heiss |
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Rok vydání: | 2001 |
Předmět: |
Cytoplasm
congenital hereditary and neonatal diseases and abnormalities Light Molecular Sequence Data Golgi Apparatus Receptors Cytoplasmic and Nuclear Peptide Plasma protein binding Biology Guanosine Diphosphate Models Biological Article General Biochemistry Genetics and Molecular Biology symbols.namesake Humans Amino Acid Sequence Enzyme Inhibitors Binding site skin and connective tissue diseases Molecular Biology Peptide sequence chemistry.chemical_classification Binding Sites Dose-Response Relationship Drug General Immunology and Microbiology General Neuroscience Membrane Proteins Intracellular Membranes COPI Golgi apparatus Recombinant Proteins Transmembrane protein Protein Structure Tertiary Cell biology Cross-Linking Reagents Membrane chemistry symbols ADP-Ribosylation Factor 1 Peptides Dimerization Thiocyanates Protein Binding |
Zdroj: | The EMBO Journal. 20:6751-6760 |
ISSN: | 1460-2075 |
Popis: | 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. |
Databáze: | OpenAIRE |
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