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DOK1 — INS
Pathways - manually collected, often from reviews:
Text-mined interactions from Literome
Noguchi et al., EMBO J 1999
:
The maximal
insulin induced tyrosine phosphorylation of
Dok required a Src family kinase ...
Insulin promoted the association of tyrosine phosphorylated
Dok with the adapter protein NCK and rasGAP
Wick et al., J Biol Chem 2001
(MAP Kinase Signaling System) :
However, mutations at Tyr ( 362 ) and Tyr ( 398 ) only partially blocked
insulin stimulated
p62(dok) tyrosine phosphorylation in cells, indicating that p62(dok) is also a target for other cellular tyrosine kinase ( s ) in addition to the IR
Sánchez-Margalet et al., Cell Mol Life Sci 2003
:
In summary, these results demonstrate that Sam68 works as a cytoplasmic
docking protein which is recruited by IR signaling and whose expression is
induced by
insulin stimulation, suggesting a putative role for Sam68 in insulin signal transduction
Csermely et al., Biochemistry 1992
:
Insulin induced the phosphorylation of seven DNA binding proteins : pp34, pp40, pp48,
pp62 , pp64, pp66, and pp72