http://purl.uniprot.org/citations/16887332 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16887332 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16887332 | http://www.w3.org/2000/01/rdf-schema#comment | "UNC-51-like kinases (ULK) are members of an evolutionarily conserved sub-family of ubiquitously expressed serine/threonine-specific protein kinases. Here we report that fibroblast growth factor receptor substrate (FRS) 2/3 are novel ULK2 carboxy-terminal domain interacting proteins. FRS2/3 are homologs that function as adaptor proteins to mediate signaling of multiple receptor tyrosine kinases. ULK2 interacts with the phospho-tyrosine binding (PTB) domain of FRS2/3. We demonstrate that siRNA targeting ULK2 in mouse P19 cells results in elevated FGFR1 mediated FRS3 and SHP2 tyrosyl phosphorylation. In addition, RNAi-mediated decrease in ULK2 causes increased interaction between FGFR1 and FRS3. ULK2 phosphorylates FRS2/3 in vitro, suggesting that ULK2 mediated phosphorylation may be a mechanism of FRS2/3 regulation. The data presented support a model in which ULK2, by interaction with FRS2/3 and inhibition of SynGAP, functions to negatively regulate tyrosyl phosphorylation of signaling proteins downstream of FGFR1."xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cellsig.2006.06.003"xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cellsig.2006.06.003"xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/author | "Figueroa C."xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/author | "Figueroa C."xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/author | "Vojtek A.B."xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/author | "Vojtek A.B."xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/author | "Avery A.W."xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/author | "Avery A.W."xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/name | "Cell. Signal."xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/name | "Cell. Signal."xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/pages | "177-184"xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/pages | "177-184"xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/title | "UNC-51-like kinase regulation of fibroblast growth factor receptor substrate 2/3."xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/title | "UNC-51-like kinase regulation of fibroblast growth factor receptor substrate 2/3."xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/volume | "19"xsd:string |
http://purl.uniprot.org/citations/16887332 | http://purl.uniprot.org/core/volume | "19"xsd:string |
http://purl.uniprot.org/citations/16887332 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16887332 |
http://purl.uniprot.org/citations/16887332 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16887332 |
http://purl.uniprot.org/citations/16887332 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16887332 |
http://purl.uniprot.org/citations/16887332 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16887332 |