ArticleMolecular biology of the cell1997
Interaction of coatomer with aminoglycoside antibiotics: evidence that coatomer has at least two dilysine binding sites.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 32 citations in OpenAlex.
- In Vitro Reconstitution of Plant COPII Vesicles.Methods in molecular biology (Clifton, N.J.) · 2024Article
- In vitro reconstitution of COPII vesicles from Arabidopsis thaliana suspension-cultured cells.Nature protocols · 2023Review
- Hygromycin B hypersensitive (hhy) mutants implicate an intact trans-Golgi and late endosome interface in efficient Tor1 vacuolar localization and TORC1 function.Current genetics · 2017Article
- Rsp5 ubiquitin ligase is required for protein trafficking in Saccharomyces cerevisiae COPI mutants.PloS one · 2012Article
- Identification of yeast genes involved in k homeostasis: loss of membrane traffic genes affects k uptake.G3 (Bethesda, Md.) · 2011Article
- Review
- Essential lysine residues within transmembrane helix 1 of diphtheria toxin facilitate COPI binding and catalytic domain entry.Molecular microbiology · 2010Article
- Genomic analysis of severe hypersensitivity to hygromycin B reveals linkage to vacuolar defects and new vacuolar gene functions in Saccharomyces cerevisiae.Current genetics · 2010Article
- COPI-mediated transport.The Journal of membrane biology · 2006Review
- RGS4 and RGS2 bind coatomer and inhibit COPI association with Golgi membranes and intracellular transport.Molecular biology of the cell · 2000Article
- Luv1p/Rki1p/Tcs3p/Vps54p, a yeast protein that localizes to the late Golgi and early endosome, is required for normal vacuolar morphology.Molecular biology of the cell · 2000Article
- Arabidopsis Sec21p and Sec23p homologs. Probable coat proteins of plant COP-coated vesicles.Plant physiology · 1999Article
- Inhibition of secretion by 1,3-Cyclohexanebis(methylamine), a dibasic compound that interferes with coatomer function.Molecular biology of the cell · 1999Article
- Receptor-induced polymerization of coatomer.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Coatomer is the soluble precursor of the COPI coat (coat protein I) involved in traffic among membranes of the endoplasmic reticulum and the Golgi apparatus. We report herein that neomycin precipitates coatomer from cell extracts and from purified coatomer preparations. Precipitation first increased and then decreased as the neomycin concentration increased, analogous to the precipitation of a polyvalent antigen by divalent antibodies. This suggested that neomycin cross-linked coatomer into large aggregates and implies that coatomer has two or more binding sites for neomycin. A variety of other aminoglycoside antibiotics precipitated coatomer, or if they did not precipitate, they interfered with the ability of neomycin to precipitate. Coatomer is know to interact with a motif (KKXX) containing adjacent lysine residues at the carboxyl terminus of the cytoplasmic domains of some membrane proteins resident in the endoplasmic reticulum. All of the antibiotics that interacted with coatomer contain at least two close amino groups, suggesting that the antibiotics might be interacting with the di-lysine binding site of coatomer. Consistent with this idea, di-lysine itself blocked the interaction of antibiotics with coatomer. Moreover, di-lysine and antibiotics each blocked the coating of Golgi membranes by coatomer. These data suggest that certain aminoglycoside antibiotics interact with di-lysine binding sites on coatomer and that coatomer contains at least two of these di-lysine binding sites.
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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.