| http://purl.uniprot.org/citations/20584982 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20584982 | http://www.w3.org/2000/01/rdf-schema#comment | "Myristoylation is critical for membrane association of Src kinases, but a role for myristate in regulating other aspects of Src biology has not been explored. In the c-Abl tyrosine kinase, myristate binds within a hydrophobic pocket at the base of the kinase domain and latches the protein into an autoinhibitory conformation. A similar pocket has been predicted to exist in c-Src, raising the possibility that Src might also be regulated by myristoylation. Here we show that in contrast to the case for c-Abl, myristoylation exerts a positive effect on c-Src kinase activity. We also demonstrate that myristoylation and membrane binding regulate c-Src ubiquitination and degradation. Nonmyristoylated c-Src exhibited reduced kinase activity but had enhanced stability compared to myristoylated c-Src. We then mutated critical residues in the predicted myristate binding pocket of c-Src. Mutation of L360 and/or E486 had no effect on c-Src membrane binding or localization. However, constructs containing a T456A mutation were partially released from the membrane, suggesting that mutagenesis could induce c-Src to undergo an artificial myristoyl switch. All of the pocket mutants exhibited decreased kinase activity. We concluded that myristoylation and the pocket residues regulate c-Src, but in a manner very different from that for c-Abl."xsd:string |
| http://purl.uniprot.org/citations/20584982 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.00246-10"xsd:string |
| http://purl.uniprot.org/citations/20584982 | http://purl.uniprot.org/core/author | "Resh M.D."xsd:string |
| http://purl.uniprot.org/citations/20584982 | http://purl.uniprot.org/core/author | "Patwardhan P."xsd:string |
| http://purl.uniprot.org/citations/20584982 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20584982 | http://purl.uniprot.org/core/name | "Mol Cell Biol"xsd:string |
| http://purl.uniprot.org/citations/20584982 | http://purl.uniprot.org/core/pages | "4094-4107"xsd:string |
| http://purl.uniprot.org/citations/20584982 | http://purl.uniprot.org/core/title | "Myristoylation and membrane binding regulate c-Src stability and kinase activity."xsd:string |
| http://purl.uniprot.org/citations/20584982 | http://purl.uniprot.org/core/volume | "30"xsd:string |
| http://purl.uniprot.org/citations/20584982 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20584982 |
| http://purl.uniprot.org/citations/20584982 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20584982 |
| http://purl.uniprot.org/uniprot/#_P41239-mappedCitation-20584982 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/20584982 |
| http://purl.uniprot.org/uniprot/#_Q90956-mappedCitation-20584982 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/20584982 |
| http://purl.uniprot.org/uniprot/Q90956 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/20584982 |
| http://purl.uniprot.org/uniprot/P41239 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/20584982 |