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AKT3 — LYN

Text-mined interactions from Literome

Li et al., Proc Natl Acad Sci U S A 1999 : Lyn inhibited Akt/PKB additively with an okadaic acid-sensitive endogenous phosphatase ( s ) ... Negative regulation of Akt/PKB by Lyn was not dependent on the protein phosphatases SHP-1, SHP-2, or SHIP
Kitaura et al., J Exp Med 2000 : Phosphorylation of Akt is regulated positively by Btk and Syk and negatively by Lyn
Cho et al., Blood 2002 : Role of the Src family kinase Lyn in TxA2 production, adenosine diphosphate secretion, Akt phosphorylation, and irreversible aggregation in platelets stimulated with gamma-thrombin
Kawauchi et al., Int J Hematol 2002 (Leukemia, Lymphocytic, Chronic, B-Cell...) : In B-CLL cells, BCR cross linking neither induced activation nor enhanced the activities of Lyn , Syk, p21ras, JNK, p38 MAPK, or Akt kinases, whereas p38 MAPK and Akt were constitutively active
Qin et al., Biochemistry 2003 : Under our conditions, hydrogen peroxide induced PI3K and Akt activation was independent of Lyn , Syk, Cbl, BCAP, or Ras when each was eliminated individually either by mutation or by a specific inhibitor
Baran et al., J Biol Chem 2003 : The inositol 5'-phosphatase SHIP-1 and the Src kinase Lyn negatively regulate macrophage colony stimulating factor induced Akt activity ... Additionally, in 3T3-Fms cells, Lyn enhanced the ability of SHIP-1 to regulate Akt activation by stabilizing SHIP-1 at the cellular membrane ... These data provide the first evidence of the involvement of both SHIP-1 and Lyn in the negative regulation of M-CSF-R induced Akt activation
Mikhalap et al., Blood 2004 (MAP Kinase Signaling System) : CD150 mediated Akt phosphorylation required Syk and SH2D1A, was negatively regulated by Lyn and Btk, but was SHIP independent
Murata et al., J Nat Med 2013 (Leukemia) : The targets of hesperetin and naringenin were found : hesperetin inhibited phosphorylation of Syk and Akt, while naringenin suppressed the expression of Lyn and inhibited the phosphorylation of Akt