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AKT1 — GRB10
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
Text-mined interactions from Literome
Jahn et al., Mol Cell Biol 2002
:
Role for the adaptor protein
Grb10 in the activation of
Akt ... We found that Akt and Grb10 form a constitutive complex, suggesting a
role for
Grb10 in the translocation of
Akt to the cell membrane ...
Grb10 induced
Akt activation was observed without increased phosphatidylinositol 3-kinase ( PI3-kinase ) activity, suggesting that Grb10 is a positive regulator of Akt downstream of PI3-kinase
Mori et al., Mol Cell Endocrinol 2005
:
In spite of these differences, both
FL-Grb10 and the BPS-SH2 fragment
inhibited insulin stimulated phosphorylation of IRS1, IRS2,
Akt/PKB , Shc, ERK1/2, APS, and c-Cbl to a similar extent ... In spite of these differences, both
FL-Grb10 and the BPS-SH2 fragment
inhibited insulin stimulated phosphorylation of IRS1, IRS2,
Akt/PKB , Shc, ERK1/2, APS, and c-Cbl to a similar extent
Wang et al., Mol Cell Biol 2007
(Body Weight) :
Loss of
Grb10 expression in insulin target tissues, such as skeletal muscle and fat,
resulted in enhanced insulin stimulated
Akt and mitogen activated protein kinase phosphorylation
Holt et al., Mol Endocrinol 2009
:
These results indicate that, in addition to their described effects on
IRS-1/Akt ,
Grb10 and Grb14 may
regulate whole-body glucose homeostasis by additional mechanisms and highlight these adaptors as potential therapeutic targets for amelioration of the insulin resistance associated with type 2 diabetes
Singh et al., J Cell Physiol 2013
:
Stimulation of
Akt by interaction with
Grb10 then activates NF-?B, which further enhances HuR mRNA and protein expression
Kazi et al., Mol Oncol 2013
:
However, expression of
Grb10 enhanced FL-induced
Akt phosphorylation without affecting Erk or p38 phosphorylation in Ba/F3-FLT3-WT and Ba/F3-FLT3-ITD