Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
Overexpression of protein tyrosine phosphatase 1B in adipocytes inhibits insulin stimulated phosphoinositide 3 kinase activity without altering glucose transport or Akt / Protein kinase B activation . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
Mechanism for differential effect of protein tyrosine phosphatase 1B on Akt versus mitogen activated protein kinase in 3T3 L 1 adipocytes . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
Here we show that protein tyrosine phosphatase 1B ( PTPIB ) activates Src , thereby initiating the activation of a Rac dependent pathway leading to cytoskeletal remodeling . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
Expression of insulin receptor , protein tyrosine phosphatase 1B ( PTP1B ) , phosphorylation of insulin receptor ( Tyr 1146 ) and Akt were evaluated by Western blot analysis . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
Reexpression of PTP 1B in spontaneously immortalized fibroblasts resulted in decreased IGF IR and AKT activation , as well as decreased protection from apoptosis and decreased motility . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
In both cells , PTP1B overexpression blocked insulin stimulated tyrosine phosphorylation of the insulin receptor and IRS 1 by more than 70 % and resulted in a significant inhibition of the association between IRS 1 and the p 85 subunit of phosphatidylinositol 3 kinase and Akt phosphorylation as well as mitogen activated protein kinase phosphorylation . ^^^ These effects were specific for insulin signaling , because platelet derived growth factor ( PDGF ) stimulated PDGF receptor tyrosine phosphorylation and Akt phosphorylation were not inhibited by PTP1B overexpression . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
Phosphorylation of PTP1B at Ser ( 50 ) by Akt impairs its ability to dephosphorylate the insulin receptor . ^^^ Interestingly , PTP1B contains this motif ( RYRDVS ( 50 ) ) , and wild type PTP1B ( but not mutants with substitutions for Ser ( 50 ) ) was significantly phosphorylated by Akt in vitro . ^^^ To determine whether PTP1B is a substrate for Akt in intact cells , NIH 3T3 ( IR ) cells transfected with either wild type PTP1B or PTP1B S50A were labeled with [ ( 32 ) P ] orthophosphate . ^^^ Insulin stimulation caused a significant increase in phosphorylation of wild type PTP1B that could be blocked by pretreatment of cells with wortmannin or cotransfection of a dominant inhibitory Akt mutant . ^^^ Cotransfection of constitutively active Akt caused robust phosphorylation of wild type PTP1B both in the absence and presence of insulin . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
However , Erk activation is enhanced only slightly , and there is no increase in Akt activation in PTP1B deficient cells . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
Reduction of PTP1B expression in FAO cells also caused an increase in insulin stimulated phosphorylation of PKB and GSK 3 , without any change in protein expression . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
Although , adipose tissue of 10 week old MSG rats showed higher PTP1B expression and IR / PTP1B interaction , they were not sufficient to impair all insulin signaling since IRS 2 phosphorylation and association with PI 3 kinase and Akt serine phosphorylation were increased , which may contribute for the increased adiposity of these animals . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
Treatment of cells with PTP1B inhibitors , both in the presence and in the absence of insulin , markedly enhances IRbeta and IRS 1 phosphorylation , Akt and ERK1 / 2 activation , Glut 4 translocation , glucose uptake , and Elk 1 transcriptional activation and cell proliferation . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
A steady state analysis indicates that negative feedback regulation of PTP1B by Akt elicits bistability in insulin stimulated GLUT 4 translocation . ^^^ CONCLUSION : A steady state analysis indicates that negative feedback regulation of phosphatase PTP1B by Akt elicits bistability in insulin stimulated GLUT 4 translocation . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
Furthermore , transfection of mouse hepatocytes with PTP1B siRNA downregulated p85alpha protein expression and enhanced insulin induced PKB phosphorylation . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
Whereas insulin induced phosphatidylinositol 3 kinase / Akt signaling was prolonged in both TCPTP / and PTP1B / immortalized mouse embryo fibroblasts ( MEFs ) , mitogen activated protein kinase ERK1 / 2 signaling was elevated only in PTP1B null MEFs . ^^^ Consistent with this , suppression of TCPTP protein levels by RNA interference in PTP1B / MEFs resulted in no change in ERK1 / 2 signaling but caused prolonged Akt activation and Y1162 / Y1163 phosphorylation . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
In addition , we demonstrated an impairment of the insulin induced IR / IRSs / PI3K / Akt pathway in liver and muscle of chronic hyperinsulinaemic rats that parallels increases in IRS1 / 2 serine phosphorylation , IR / PTP1B association and mTOR activity . ^^^ Despite a higher association of IR / PTP1B , there was an increase in white adipose tissue of chronic hyperinsulinaemic rats in IRS 1 / 2 protein levels , tyrosine phosphorylation and IRSs / PI3K association , which led to an increase in basal Akt serine phosphorylation . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
Protein kinase B ( PKB ) serine phosphorylation was increased sevenfold in liver of PTP1B ASO treated mice upon insulin stimulation , while phosphorylation of PKB substrates , glycogen synthase kinase ( GSK ) 3alpha and 3beta , was increased more than twofold . ^^^ Peripheral insulin signaling was increased by PTP1B ASO , as evidenced by increased phosphorylation of PKB in muscle of insulin stimulated PTP1B ASO treated animals despite the lack of measurable effects on muscle PTP1B protein . ^^^ Protein kinase B ( PKB ) serine phosphorylation was increased sevenfold in liver of PTP1B ASO treated mice upon insulin stimulation , while phosphorylation of PKB substrates , glycogen synthase kinase ( GSK ) 3alpha and 3beta , was increased more than twofold . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
The ortho substitution to the ( S ) IZD on the aryl ring afforded low nanomolar enzyme inhibitors of PTP1B that also displayed low caco 2 permeability and cellular activity in an insulin receptor ( IR ) phosphorylation assay and an Akt phosphorylation assay . ^^^
Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
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Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
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Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
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Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
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Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
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Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
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Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
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Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
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Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
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Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
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Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
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Interacting proteins: P18031 and P31749 Pubmed SVM Score :0.0
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