sub:provenance {
  beldoc: dce:description "Approximately 61,000 statements." ;
    dce:rights "Copyright (c) 2011-2012, Selventa. All rights reserved." ;
    dce:title "BEL Framework Large Corpus Document" ;
    pav:authoredBy sub:_6 ;
    pav:version "1.4" .
  sub:_5 prov:value "Binding of dimerized KitL induces the dimerization of Kit [32]. This leads to the autophosphorylation of Kit on tyrosine and its association with substrates of various kinds. The phophatidylinositol-3-kinase (PI3K)/Akt system is one of the major pathways [33] (fig. 1). PI3K is composed of an 85-kDa regulatory subunit and a 110-kDa catalytic subunit. The 85-kDa regulatory subunit is associated with activated Kit through an SH2 domain, and then is phosphorylated on tyrosine. The 110-kDa catalytic subunit of the activated PI3K produces phosphatidylinositol-3,4-bisphosphate, which in turn is used for phosphorylation of Akt, a serine-threonine kinase. The activated Akt is involved in the inhibition of apoptosis of cells whose survival depends on Kit signaling. A tyrosine kinase inhibitor, imatinib mesylate blocks not only autophosphorylation of Kit but also phosphorylation of Akt [34]. Induction of apoptosis in Kit signaling-dependent cells by imatinib mesylate may be mediated through the inhibition of Akt activity." ;
    prov:wasQuotedFrom pubmed:15583854 .
  sub:_6 rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:15583854 ;
    prov:wasDerivedFrom beldoc: , sub:_5 .
}