Source:http://linkedlifedata.com/resource/pubmed/id/17506542
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7
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| pubmed:dateCreated |
2007-7-6
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| pubmed:abstractText |
Following stimulation of NRK49F rat kidney fibroblast cells with epidermal growth factor, possible preemptive cross-talk between arginine methylation and serine and tyrosine phosphorylation was observed for Rho guanidine nucleotide dissociation inhibitor 1 (RhoGDI-1). Five dimethylation sites (Lys50, Lys52, Arg111, Arg152, Arg180) and two new phosphorylation sites (Tyr144, Ser148) were identified for RhoGDI-1. All presently known phosphorylation sites for RhoGDI-1 lie within the 10 residues immediately prior to the 3 sites for arginine dimethylation, and these dimethylation/phosphorylation modules may constitute functional switches. Consideration of structural data and other literature for RhoGDI-1 suggests that methylation and phosphorylation cooperatively affect formation of complexes with different Rho/Rac family proteins and that methylation may be crucial in partitioning of RhoGDI-1 between different functional roles. On the basis of results presented here, it can be implied that unidentified arginine methyltransferases may exist and that arginine methylation may have a greater role in cellular signaling processes than is currently recognized. The combined use of SILAC labeling of arginine (SILAC = stable isotope labeling by amino acids in cell culture), immobilized metal affinity chromatography based phosphoprotein enrichment, and mass spectrometry is clearly a useful method for this investigation.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Dissociation...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/cdc42 GTP-Binding Protein,
http://linkedlifedata.com/resource/pubmed/chemical/rho guanine nucleotide...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
1535-3893
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
6
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
2623-30
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| pubmed:meshHeading |
pubmed-meshheading:17506542-Amino Acid Sequence,
pubmed-meshheading:17506542-Amino Acids,
pubmed-meshheading:17506542-Animals,
pubmed-meshheading:17506542-Arginine,
pubmed-meshheading:17506542-Cell Line,
pubmed-meshheading:17506542-Chromatography, Affinity,
pubmed-meshheading:17506542-Epidermal Growth Factor,
pubmed-meshheading:17506542-Fibroblasts,
pubmed-meshheading:17506542-Guanine Nucleotide Dissociation Inhibitors,
pubmed-meshheading:17506542-Isotope Labeling,
pubmed-meshheading:17506542-Methylation,
pubmed-meshheading:17506542-Molecular Sequence Data,
pubmed-meshheading:17506542-Phosphopeptides,
pubmed-meshheading:17506542-Phosphoproteins,
pubmed-meshheading:17506542-Phosphorylation,
pubmed-meshheading:17506542-Protein Conformation,
pubmed-meshheading:17506542-Protein Processing, Post-Translational,
pubmed-meshheading:17506542-Proteomics,
pubmed-meshheading:17506542-Rats,
pubmed-meshheading:17506542-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:17506542-cdc42 GTP-Binding Protein
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| pubmed:year |
2007
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| pubmed:articleTitle |
Proteomics study reveals cross-talk between Rho guanidine nucleotide dissociation inhibitor 1 post-translational modifications in epidermal growth factor stimulated fibroblasts.
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| pubmed:affiliation |
Department of Medicine, University College London, 5 University Street, London.
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| pubmed:publicationType |
Journal Article
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