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http://purl.uniprot.org/citations/20719962http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20719962http://www.w3.org/2000/01/rdf-schema#comment"Sprouty (Spry) proteins are negative regulators of receptor tyrosine kinase signaling; however, their exact mechanism of action remains incompletely understood. We identified phosphatidylinositol-specific phospholipase C (PLC)-γ as a partner of the Spry1 and Spry2 proteins. Spry-PLCγ interaction was dependent on the Src homology 2 domain of PLCγ and a conserved N-terminal tyrosine residue in Spry1 and Spry2. Overexpression of Spry1 and Spry2 was associated with decreased PLCγ phosphorylation and decreased PLCγ activity as measured by production of inositol (1,4,5)-triphosphate (IP(3)) and diacylglycerol, whereas cells deficient for Spry1 or Spry1, -2, and -4 showed increased production of IP(3) at baseline and further increased in response to growth factor signals. Overexpression of Spry 1 or Spry2 or small-interfering RNA-mediated knockdown of PLCγ1 or PLCγ2 abrogated the activity of a calcium-dependent reporter gene, suggesting that Spry inhibited calcium-mediated signaling downstream of PLCγ. Furthermore, Spry overexpression in T-cells, which are highly dependent on PLCγ activity and calcium signaling, blocked T-cell receptor-mediated calcium release. Accordingly, cultured T-cells from Spry1 gene knockout mice showed increased proliferation in response to T-cell receptor stimulation. These data highlight an important action of Spry, which may allow these proteins to influence signaling through multiple receptors."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e10-02-0123"xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Aggarwal P."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Collins S."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Powell J."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Kim M.K."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Phillips M."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Licht J.D."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Quatela S."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Reddi A.L."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Ambardekar C."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Mason J."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Basson M.A."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Vilimas T."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Akbulut S."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Lovatt M."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Canciani B."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/author"Hix L."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/name"Mol Biol Cell"xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/pages"3487-3496"xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/title"Sprouty proteins inhibit receptor-mediated activation of phosphatidylinositol-specific phospholipase C."xsd:string
http://purl.uniprot.org/citations/20719962http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/20719962http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20719962