Insulin stimulates PKCzeta -mediated phosphorylation of insulin receptor substrate-1 (IRS-1). A self-attenuated mechanism to negatively regulate the function of IRS proteins (Q24291007)

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English	Insulin stimulates PKCzeta -mediated phosphorylation of insulin receptor substrate-1 (IRS-1). A self-attenuated mechanism to negatively regulate the function of IRS proteins	scientific article

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Continued use of retracted papers: Temporal trends in citations and (lack of) awareness of retractions shown in citation contexts in biomedicine

Insulin stimulates PKCzeta -mediated phosphorylation of insulin receptor substrate-1 (IRS-1). A self-attenuated mechanism to negatively regulate the function of IRS proteins (English)

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phosphorylation

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author name string

Y F Liu

1

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K Paz

2

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A Herschkovitz

3

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A Alt

4

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T Tennenbaum

5

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S R Sampson

6

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M Ohba

7

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T Kuroki

8

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D LeRoith

9

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Y Zick

10

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language of work or name

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publication date

27 April 2001

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Journal of Biological Chemistry

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276

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14459-65

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17

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Protein-protein interaction in insulin signaling and the molecular mechanisms of insulin resistance

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Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein

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Role of IRS-2 in insulin and cytokine signalling

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The 60-kDa phosphotyrosine protein in insulin-treated adipocytes is a new member of the insulin receptor substrate family.

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A novel 160-kDa phosphotyrosine protein in insulin-treated embryonic kidney cells is a new member of the insulin receptor substrate family

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Pleckstrin domain homology

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A putative modular domain present in diverse signaling proteins

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Protein modules and signalling networks

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Insulin receptor substrate-2 binds to the insulin receptor through its phosphotyrosine-binding domain and through a newly identified domain comprising amino acids 591-786

1 reference

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PTB domains of IRS-1 and Shc have distinct but overlapping binding specificities

1 reference

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Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor

1 reference

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Interaction between the insulin receptor and its downstream effectors. Use of individually expressed receptor domains for structure/function analysis

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Phosphorylation of insulin receptor substrate-1 on multiple serine residues, 612, 632, 662, and 731, modulates insulin action

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Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signaling pathway

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Activation of p70/p85 S6 kinase by a pathway independent of p21ras

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3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro

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A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphory

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Modulation of insulin receptor substrate-1 tyrosine phosphorylation and function by mitogen-activated protein kinase

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Modulation of insulin receptor substrate-1 tyrosine phosphorylation by an Akt/phosphatidylinositol 3-kinase pathway

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Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK

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Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes

1 reference

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Protein kinase C-zeta as a downstream effector of phosphatidylinositol 3-kinase during insulin stimulation in rat adipocytes. Potential role in glucose transport

1 reference

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Activation of protein kinase C (alpha, beta, and zeta) by insulin in 3T3/L1 cells. Transfection studies suggest a role for PKC-zeta in glucose transport

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Galectin-8. A new rat lectin, related to galectin-4

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Tyrosine phosphorylation of insulin receptor substrate-1 in vivo depends upon the presence of its pleckstrin homology region

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Efficient generation of recombinant adenoviruses using adenovirus DNA-terminal protein complex and a cosmid bearing the full-length virus genome

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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PDGF- and insulin-dependent pp70S6k activation mediated by phosphatidylinositol-3-OH kinase

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Requirement of atypical protein kinase clambda for insulin stimulation of glucose uptake but not for Akt activation in 3T3-L1 adipocytes

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In vivo adenoviral delivery of recombinant human protein kinase C-zeta stimulates glucose transport activity in rat skeletal muscle

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Protein kinase C: structure, function, and regulation

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Protein kinase C-zeta phosphorylates insulin receptor substrate-1 and impairs its ability to activate phosphatidylinositol 3-kinase in response to insulin.

1 reference

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Activation of IkappaB kinase beta by protein kinase C isoforms

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Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase

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p70 S6 kinase is regulated by protein kinase Czeta and participates in a phosphoinositide 3-kinase-regulated signalling complex

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Requirement for protein-tyrosine phosphatase SHP-2 in insulin-induced activation of c-Jun NH(2)-terminal kinase

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Inhibition of MAP Kinase Kinase Blocks the Differentiation of PC-12 Cells Induced by Nerve Growth Factor

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PKC zeta is a molecular switch in signal transduction of TNF-alpha, bifunctionally regulated by ceramide and arachidonic acid

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Insulin differentially regulates SAPKs/JNKs and ERKs in CHO cells overexpressing human insulin receptors

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Phosphorylation of insulin receptor substrate-1 (IRS-1) by protein kinase B positively regulates IRS-1 function

1 reference

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Signaling mechanisms that regulate glucose transport

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Molecular basis of insulin-stimulated GLUT4 vesicle trafficking. Location! Location! Location!

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Identifiers

10.1074/JBC.M007281200

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