ArticleBiophysical journal2006
Insertion of lipidated Ras proteins into lipid monolayers studied by infrared reflection absorption spectroscopy (IRRAS).
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Chemical approaches for investigating site-specific protein S-fatty acylation.Current opinion in chemical biology · 2021Review
- Measuring protein insertion areas in lipid monolayers by fluorescence correlation spectroscopy.Biophysical journal · 2021Article
- Article
- EHD2 restrains dynamics of caveolae by an ATP-dependent, membrane-bound, open conformation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Mechanisms of membrane binding of small GTPase K-Ras4B farnesylated hypervariable region.The Journal of biological chemistry · 2015Article
- H-Ras forms dimers on membrane surfaces via a protein-protein interface.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Human islet amyloid polypeptide at the air-aqueous interface: a Langmuir monolayer approach.Journal of the Royal Society, Interface · 2012Article
- The role of G-domain orientation and nucleotide state on the Ras isoform-specific membrane interaction.European biophysics journal : EBJ · 2012Article
- Influence of the lipid anchor motif of N-ras on the interaction with lipid membranes: a surface plasmon resonance study.Biophysical journal · 2010Article
- Ranaspumin-2: structure and function of a surfactant protein from the foam nests of a tropical frog.Biophysical journal · 2009Article
- Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy.Biophysical journal · 2007Article
- H-ras protein in a bilayer: interaction and structure perturbation.Journal of the American Chemical Society · 2007Article
- Ras nanoclusters: molecular structure and assembly.Seminars in cell & developmental biology · 2007Review
- Determination of the contribution of the myristoyl group and hydrophobic amino acids of recoverin on its dynamics of binding to lipid monolayers.Biophysical journal · 2007Article
- Membrane binding of a lipidated N-Ras protein studied in lipid monolayers.European biophysics journal : EBJ · 2007Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ras proteins have to be associated with the inner leaflet of the plasma membrane to perform their signaling functions. This membrane targeting and binding is controlled by post-translational covalent attachment of farnesyl and palmitoyl chains to cysteines in the membrane anchor region of the N- and H-Ras isoforms. Two N-Ras lipoproteins were investigated, namely a farnesylated and hexadecylated protein, presenting the natural hydrophobic modifications and a doubly hexadecylated construct, respectively. The proteins are surface active and form a Gibbs monolayer at the air-D2O interface. The contours of the amide-I bands were analyzed using infrared reflection absorption spectroscopy (IRRAS). Langmuir monolayers of a mixture of POPC, brain sphingomyelin, and cholesterol were used as half of a model biomembrane to study the insertion of these N-Ras proteins. They insert with their hydrophobic anchors into lipid monolayers but at higher surface pressures (30 mN/m); the farnesylated and hexadecylated protein desorbs completely from the monolayer, whereas the doubly hexadecylated protein remains incorporated. During the insertion process, changes in the orientation of the protein secondary structure were detected by comparison with simulated IRRA spectra, based on the information on the relative orientation of the secondary structure elements from the protein crystal structure data.
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