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ARHGEF7 — INS

Text-mined interactions from Literome

Andreelli et al., Diabetologia 1999 (Diabetes Mellitus...) : In contrast, insulin increased p85alpha-phosphatidylinositol-3-kinase mRNA expression in muscle from non-diabetic subjects ( +98+/-22 % in lean and +127+/-16 % in obese, p < 0.02 ) but this effect was totally impaired in Type II diabetic patients ( +5+/-12 %, NS )
Chen et al., Mol Cell Biol 1999 : Furthermore, there was no effect on either the insulin stimulated association of the p85 type I phosphatidylinositol (PI) 3-kinase regulatory subunit with IRS1 or phosphotyrosine antibody immunoprecipitated PI 3-kinase activity
Shao et al., J Endocrinol 2000 (Diabetes Mellitus, Experimental...) : The level of insulin stimulated tyrosine phosphorylation of p85alpha from phosphatidylinositol 3 (PI 3)-kinase, which is upstream of Akt, was also reduced in muscle and adipose tissue from db/db mice ( P < 0.05 ) ; however, there was no change in extracellular signal regulated kinase-1 or -2 phosphorylation
Janez et al., Endocrinology 2000 (Insulin Resistance) : Furthermore, chronic insulin exposure led to a marked impairment in the ability of Gab-1 to associate with p85 subunit of PI 3-kinase in response to acute shock and insulin stimulation
Conejo et al., J Cell Physiol 2001 (MAP Kinase Signaling System) : Insulin stimulated IRS-1 association with p85alpha leading to the activation of PI3-kinase, and, subsequently AKT and p70S6-kinases
Najib et al., J Mol Endocrinol 2001 : A 10 min exposure to homocysteine thiolactone ( 50 microM ) resulted in a significant inhibition of insulin stimulated tyrosine phosphorylation of the insulin receptor beta-subunit and its substrates IRS-1 and p60-70, as well as their association with the p85 regulatory subunit of phosphatidylinositol 3-kinase
Ueki et al., Proc Natl Acad Sci U S A 2002 : These results indicate that in addition to their roles in recruiting the catalytic subunit of PI3K to the insulin receptor substrate proteins, both p85alpha and p85beta play negative roles in insulin signaling
Dominici et al., J Endocrinol 2002 (Growth Disorders) : The insulin stimulated association of the p85 regulatory subunit of phosphatidylinositol (PI) 3-kinase with IRS-1 was increased by 28 %, but unaltered with IRS-2
Hirose et al., Br J Pharmacol 2002 : Lignocaine reduced insulin stimulated tyrosine phosphorylation of IR-beta to 12.6+/-5.7 % ( P < 0.001 ), and IRS-1 to 32.1+/-18.8 % ( P < 0.01 ), and also reduced insulin stimulated binding of IRS-1 to p85 to 27.4+/-12.7 % ( P < 0.001 ) relative to control ( 100 % ) in muscle in vivo
Shah et al., Biochem J 2002 : In the present study, we have shown that 4-amino-5- ( 4-methylphenyl ) -7- ( t-butyl ) pyrazolo [ 3,4-d ] pyrimidine ( PP1 ), a selective inhibitor of the Src family of non-receptor tyrosine kinases, interferes with the activation of 70 and 85 kDa S6K gene products ( p70S6K1 and p85S6K1 ) by insulin , insulin-like growth factor 1, sodium orthovanadate and activated alleles of phosphoinositide 3-kinase and H-Ras
Cui et al., Mol Endocrinol 2002 : AT2 receptor stimulation did not change insulin induced tyrosine phosphorylation of IRS-2 or its association with the p85alpha subunit of PI3K, but led to a significant reduction of insulin induced p85alpha phosphorylation
Kraus et al., J Endocrinol 2002 : Insulin induced insulin receptor substrate-1 tyrosine phosphorylation and binding to the regulatory subunit p85 of phosphatidylinositol 3-kinase ( PI 3-kinase ) were diminished by approximately 60 % and 40 %, respectively
Senn et al., Diabetes 2002 (Insulin Resistance) : The IL-6 effect is characterized by a decreased tyrosine phosphorylation of IR substrate (IRS)-1 and decreased association of the p85 subunit of phosphatidylinositol 3-kinase with IRS-1 in response to physiologic insulin levels
Chodniewicz et al., Blood 2003 : In contrast, insulin did not increase p85 phosphorylation and did not enhance PI3K activity or PtdIns ( 3,4,5 ) P3 production
Arribas et al., J Biol Chem 2003 : In brown adipocytes expressing the IRS-3F4 mutant, the association of the p85alpha regulatory subunit via Src homology 2 binding was lost, but insulin nevertheless induced PI 3-kinase activity and Akt phosphorylation in a wortmannin dependent manner
Yonezawa et al., J Biol Chem 1992 : Insulin also induced an association of p85 with the tyrosine phosphorylated insulin receptor substrate 1 (IRS-1) and other phosphorylated proteins ranging in size from 100 to 170 kDa but not with the activated insulin receptor
Desrois et al., Cardiovasc Res 2004 (Diabetes Mellitus, Type 2) : Owing to the decreased IRS-1 protein levels, GK rat hearts had a 41 % ( p < 0.0001 ) decrease in insulin stimulated IRS-1 protein association with the p85 subunit of phosphatidylinositol 3-kinase, despite normal phosphatidylinositol 3-kinase protein expression
Li et al., J Biol Chem 2004 : In contrast, SOCS-6 associated p85 was not degraded and could be recruited to the newly synthesized SOCS-6 molecules in the presence of insulin, suggesting that SOCS-6 expression and its interaction with p85 , but not the degradation, is regulated by insulin
O'keefe et al., Metabolism 2004 (Insulin Resistance) : The activities of these proteins were also unchanged, as insulin stimulated IR-beta tyrosine phosphorylation, IRS-1 tyrosine phosphorylation, IRS-1 associated p85 , and Akt serine phosphorylation were similar to controls
Brennesvik et al., Cell Signal 2005 : These effects were inhibited by wortmannin but adrenaline did not increase insulin stimulated p85alpha PI 3-kinase activity
Argentino et al., Horm Metab Res 2005 (Body Weight...) : We measured insulin stimulated phosphorylation of the IR and IRS-1, IRS-1-p85 association and Akt activation, and the abundance of the IR, IRS-1, p85 , GLUT-4 and IGF-1 receptor in skeletal muscle
Haasch et al., Biochem Biophys Res Commun 2006 (Insulin Resistance) : To investigate whether an increase in PKCtheta expression leads to insulin resistance, C2C12 skeletal muscle cells were transfected with PKCtheta DNA and treated with different concentrations of insulin for 10 min. PKCtheta overexpression induced reduction of IRS-1 protein levels with a decrease in insulin induced p85 binding to IRS-1, phosphorylation of PKB and its substrates, p70 and GSK3
Bertola et al., J Biol Chem 2007 (Insulin Resistance) : HGF enhanced the tyrosine phosphorylation of Gab1, leading to the recruitment of the p85 regulated subunit of PI 3-kinase, whereas p85 was exclusively recruited by IRS1 in response to insulin
Luo et al., Endocrinology 2007 : Cells expressing the Ser ( 629 ) Ala mutation, along with increased Ser ( 636 ) phosphorylation, had decreased insulin stimulated association of the p85 regulatory subunit of phosphatidylinositol 3'-kinase with IRS-1 and decreased phosphorylation of Akt at Ser ( 473 )
Kavanaugh et al., Biochemistry 1994 : Therefore, p85 may be regulated differently by PDGF and insulin
Kelly et al., J Biol Chem 1993 : In contrast, insulin increased the association of p85 with IRS-1, the tyrosyl phosphorylation of the IRS-1 associated with p85, and the total activity of PI 3-kinase in the plasma membranes and low density membranes
Yamauchi et al., J Biol Chem 1993 : Expression of the p85 subunit inhibited the insulin stimulation of SRE-Luc activity without affecting v-Ras or v-Raf activation
Ricort et al., Eur J Biochem 1996 : Furthermore, insulin induced the translocation of p85 from the cytosol to LDM and the translocation of IRS 1 from LDM to the cytosol
Anai et al., Diabetes 1999 (Insulin Resistance) : In the liver of high-fat fed rats, insulin increased the PI 3-kinase regulatory subunit p85alpha and the PI 3-kinase activities associated with IRS-1 3.6- and 2.4-fold, and with IRS-2, 4.7- and 3.0-fold, respectively, compared with those in control rats