Matches in Nanopublications for { <http://www.tkuhn.ch/bel2nanopub/RA7sg4sAWJ8n_G55tpkgJYoWN9yqSuSn1nz8SCFqAZrBc#_5> ?p ?o ?g. }
Showing items 1 to 2 of
2
with 100 items per page.
- _5 value "Src, Lyn and Lck tyrosine kinases phosphorylate DAPP1 at Tyr(139) in vitro at similar rates in the presence or absence of PtdIns(3,4,5)P(3), and overexpression of these kinases in HEK-293 cells induces the phosphorylation of Tyr(139). co-expression of DAPP1 with Src, Lyn or Lck induced a very high level of phosphorylation of DAPP1 at Tyr139, even in unstimulated cells, which was not increased further by agonist stimulation of cells. As Src-family kinases activate the PI 3-kinase pathway in many cells [1], it is possible that the overexpression of Src, Lyn or Lck in HEK-293 cells induces the activation of PI 3-kinase, thereby promoting DAPP1 phosphorylation in unstimulated cells. As Src-family tyrosine kinases are located at the plasma membrane by virtue of myristoylation and palmitoylation of their N-termini [26], it is likely that the role of PtdIns(3,4,5)P3 is to recruit DAPP1 to the cell membrane, where it can be phosphorylated with Src-family tyrosine kinases." provenance.
- _5 wasQuotedFrom 10880360 provenance.