| http://purl.uniprot.org/citations/16166082 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16166082 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16166082 | http://www.w3.org/2000/01/rdf-schema#comment | "Protein-protein interactions have emerged as an important mechanism providing for specificity in cellular signal transduction. Two splice variants of type I cGMP-dependent protein kinase (PKG Ialpha and Ibeta) differ only in their N-terminal approximately 100 amino acids, which mediate binding to different target proteins. PKG Ibeta, but not Ialpha, binds to the general transcriptional regulator TFII-I and the inositol 1,4,5-trisphosphate receptor-associated PKG substrate IRAG. Using a combination of site-directed mutagenesis and in vitro binding assays, we identified a group of acidic amino acids in the N-terminal leucine zipper dimerization domain of PKG Ibeta required for its binding to both TFII-I and IRAG. Small clusters of basic amino acids in possible alpha-helical regions in TFII-I and IRAG were found to mediate their interaction with PKG Ibeta. Mutation of two negatively charged residues in the PKG Ibeta leucine zipper (D26K/E31R) to positively charged residues, found in corresponding positions in PKG Ialpha, completely abrogated binding to TFII-I and IRAG without disrupting PKG dimerization. Mutation of specific basic residues in TFII-I or IRAG abolished binding of the full-length proteins to PKG Ibeta in intact cells. Based on these results, we propose a model for specific PKG Ibeta interaction with target proteins."xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m507021200"xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m507021200"xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/author | "Boss G.R."xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/author | "Boss G.R."xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/author | "Casteel D.E."xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/author | "Casteel D.E."xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/author | "Pilz R.B."xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/author | "Pilz R.B."xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/pages | "38211-38218"xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/pages | "38211-38218"xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/title | "Identification of the interface between cGMP-dependent protein kinase Ibeta and its interaction partners TFII-I and IRAG reveals a common interaction motif."xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/title | "Identification of the interface between cGMP-dependent protein kinase Ibeta and its interaction partners TFII-I and IRAG reveals a common interaction motif."xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/volume | "280"xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://purl.uniprot.org/core/volume | "280"xsd:string |
| http://purl.uniprot.org/citations/16166082 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16166082 |
| http://purl.uniprot.org/citations/16166082 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16166082 |
| http://purl.uniprot.org/citations/16166082 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16166082 |
| http://purl.uniprot.org/citations/16166082 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16166082 |