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http://purl.uniprot.org/citations/8749393http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8749393http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8749393http://www.w3.org/2000/01/rdf-schema#comment"

Background

Mammalian phosphoinositide 3-kinases (PI 3-kinases) are involved in receptor-mediated signal transduction and have been implicated in processes such as transformation and mitogenesis through their role in elevating cellular phosphatidylinositol (3,4,5)-trisphosphate. Additionally, a PI 3-kinase activity which generates phosphatidylinositol 3-phosphate has been shown to be required for protein trafficking in yeast.

Results

We have identified a family of three distinct PI 3-kinases in Drosophila, using an approach based on the polymerase chain reaction to amplify a region corresponding to the conserved catalytic domain of PI 3-kinases. One of these family members, PI3K_92D, is closely related to the prototypical PI 3-kinase, p110 alpha; PI3K_59F is homologous to Vps34p, whereas the third, PI3K_68D, is a novel PI 3-kinase which is widely expressed throughout the Drosophila life cycle. The PI3K_68D cDNA encodes a protein of 210 kDa, which lacks sequences implicated in linking p110 PI 3-kinases to p85 adaptor proteins, but contains an amino-terminal proline-rich sequence, which could bind to SH3 domains, and a carboxy-terminal C2 domain. Biochemical analyses demonstrate that PI3K_68D has a novel substrate specificity in vitro, restricted to phosphatidylinositol and phosphatidylinositol 4-phosphate, and is unable to phosphorylate phosphatidylinositol (4,5)-bisphosphate, the implied in vivo substrate for p110.

Conclusions

A family of PI 3-kinases in Drosophila, including a novel class represented by PI3K_68D, is described. PI3K_68D has the potential to bind to signalling molecules containing SH3 domains, lacks p85-adaptor-binding sequences, has a Ca(2+)-independent phospholipid-binding domain and displays a restricted in vitro substrate specificity, so it could define a novel signal transduction pathway."xsd:string
http://purl.uniprot.org/citations/8749393http://purl.org/dc/terms/identifier"doi:10.1016/S0960-9822(95)00278-8"xsd:string
http://purl.uniprot.org/citations/8749393http://purl.org/dc/terms/identifier"doi:10.1016/s0960-9822(95)00278-8"xsd:string
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/author"Waterfield M.D."xsd:string
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/author"Waterfield M.D."xsd:string
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/author"Domin J."xsd:string
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/author"Domin J."xsd:string
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/author"MacDougall L.K."xsd:string
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/author"MacDougall L.K."xsd:string
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/name"Curr. Biol."xsd:string
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/name"Curr Biol"xsd:string
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/pages"1404-1415"xsd:string
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/pages"1404-1415"xsd:string
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/title"A family of phosphoinositide 3-kinases in Drosophila identifies a new mediator of signal transduction."xsd:string
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/title"A family of phosphoinositide 3-kinases in Drosophila identifies a new mediator of signal transduction."xsd:string
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/8749393http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/8749393http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8749393
http://purl.uniprot.org/citations/8749393http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8749393
http://purl.uniprot.org/citations/8749393http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8749393
http://purl.uniprot.org/citations/8749393http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8749393
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