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http://purl.uniprot.org/citations/22721555http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22721555http://www.w3.org/2000/01/rdf-schema#comment"K-Ras4B is a small GTPase whose selective membrane localization and clustering into microdomains are mediated by its polybasic farnesylated C-terminus. The importance of the subcellular distribution for the signaling activity of K-Ras4B became apparent from recent in vivo studies, showing that the delta subunit of cGMP phosphodiesterase (PDEδ), which possesses a hydrophobic prenyl-binding pocket, is able to function as a potential binding partner for farnesylated proteins, thereby leading to a modulation of the spatiotemporal organization of K-Ras. Even though PDEδ has been suggested to serve as a cytosolic carrier for Ras, the functional transport mechanism still remains largely elusive. In this study, the effect of PDEδ on the interaction of GDP- and GTP-loaded K-Ras4B with neutral and anionic model biomembranes has been investigated by a combination of different spectroscopic and imaging techniques. The results show that PDEδ is not able to extract K-Ras4B from membranes. Rather, the K-Ras4B/PDEδ complex formed in bulk solution turned out to be unstable in the presence of heterogeneous membranes, resulting in a release of farnesylated K-Ras4B upon membrane contact. With the additional observation of enhanced membrane affinity for the K-Ras4B/PDEδ complex, a molecular mechanism for the PDEδ-K-Ras4B-membrane interaction could be proposed. This includes an effective delivery of PDEδ-solubilized K-Ras4B to the plasma membrane, probably through cytoplasmic diffusion, the dissociation of the K-Ras4B/PDEδ complex upon plasma membrane contact, and finally the membrane binding of released farnesylated K-Ras4B that leads to K-Ras4B-enriched microdomain formation."xsd:string
http://purl.uniprot.org/citations/22721555http://purl.org/dc/terms/identifier"doi:10.1021/ja305518h"xsd:string
http://purl.uniprot.org/citations/22721555http://purl.uniprot.org/core/author"Kapoor S."xsd:string
http://purl.uniprot.org/citations/22721555http://purl.uniprot.org/core/author"Waldmann H."xsd:string
http://purl.uniprot.org/citations/22721555http://purl.uniprot.org/core/author"Winter R."xsd:string
http://purl.uniprot.org/citations/22721555http://purl.uniprot.org/core/author"Zimmermann G."xsd:string
http://purl.uniprot.org/citations/22721555http://purl.uniprot.org/core/author"Triola G."xsd:string
http://purl.uniprot.org/citations/22721555http://purl.uniprot.org/core/author"Weise K."xsd:string
http://purl.uniprot.org/citations/22721555http://purl.uniprot.org/core/author"Mobitz S."xsd:string
http://purl.uniprot.org/citations/22721555http://purl.uniprot.org/core/author"Werkmuller A."xsd:string
http://purl.uniprot.org/citations/22721555http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22721555http://purl.uniprot.org/core/name"J Am Chem Soc"xsd:string
http://purl.uniprot.org/citations/22721555http://purl.uniprot.org/core/pages"11503-11510"xsd:string
http://purl.uniprot.org/citations/22721555http://purl.uniprot.org/core/title"Dissociation of the K-Ras4B/PDEdelta complex upon contact with lipid membranes: membrane delivery instead of extraction."xsd:string
http://purl.uniprot.org/citations/22721555http://purl.uniprot.org/core/volume"134"xsd:string
http://purl.uniprot.org/citations/22721555http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22721555
http://purl.uniprot.org/citations/22721555http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22721555
http://purl.uniprot.org/uniprot/#_O43924-mappedCitation-22721555http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22721555
http://purl.uniprot.org/uniprot/#_P01116-mappedCitation-22721555http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22721555
http://purl.uniprot.org/uniprot/#_P0DP23-mappedCitation-22721555http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22721555
http://purl.uniprot.org/uniprot/O43924http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22721555
http://purl.uniprot.org/uniprot/P01116http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22721555
http://purl.uniprot.org/uniprot/P0DP23http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22721555