14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner (Q28235588)

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scientific article (publication date: 25 April 1997)

Language	Label	Description	Also known as
English	14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner	scientific article (publication date: 25 April 1997)

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scholarly article

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14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner (English)

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1 reference

based on heuristic

inferred from title

3

object named as

T A Gustafson

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author name string

A Craparo

1

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R Freund

2

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language of work or name

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publication date

25 April 1997

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Journal of Biological Chemistry

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272

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17

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11663-9

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IRS-1: essential for insulin- and IL-4-stimulated mitogenesis in hematopoietic cells

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Role of IRS-1-GRB-2 complexes in insulin signaling

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Insulin receptor substrate 1 is required for insulin-mediated mitogenic signal transduction

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Involvement of Src-homology/collagen (SHC) proteins in signaling through the insulin receptor and the insulin-like-growth-factor-I-receptor

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Involvement of Shc in insulin- and epidermal growth factor-induced activation of p21ras

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Effect of mutations at serines 1280-1283 on the mitogenic and transforming activities of the insulin-like growth factor I receptor

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14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteins

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Activation of Raf-1 by 14-3-3 proteins

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Interaction of the protein kinase Raf-1 with 14-3-3 proteins

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Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation

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Association of the protein kinases c-Bcr and Bcr-Abl with proteins of the 14-3-3 family

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Association of polyomavirus middle tumor antigen with 14-3-3 proteins

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Inhibition of phosphatidylinositol 3-kinase activity by association with 14-3-3 proteins in T cells

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Activation-modulated association of 14-3-3 proteins with Cbl in T cells

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14-3-3 proteins associate with cdc25 phosphatases

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Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways

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Crystal structure of the zeta isoform of the 14-3-3 protein

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Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine

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Dissociation of mitogenesis and transforming activity by C-terminal truncation of the insulin-like growth factor-I receptor

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Fused protein domains inhibit DNA binding by LexA

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Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2

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Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites

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High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier

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Non-SH2 domains within insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor I receptor

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Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain

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Characterization of an interaction between insulin receptor substrate 1 and the insulin receptor by using the two-hybrid system

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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Interaction of insulin receptor substrate-2 (IRS-2) with the insulin and insulin-like growth factor I receptors. Evidence for two distinct phosphotyrosine-dependent interaction domains within IRS-2

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Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose

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Distinct modes of interaction of SHC and insulin receptor substrate-1 with the insulin receptor NPEY region via non-SH2 domains

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Interaction of a GRB-IR splice variant (a human GRB10 homolog) with the insulin and insulin-like growth factor I receptors. Evidence for a role in mitogenic signaling

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14-3-3: modulators of signaling proteins?

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Multisite serine phosphorylation of the insulin and IGF-I receptors in transfected cells

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Catalysis of serine and tyrosine autophosphorylation by the human insulin receptor

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Expression of the insulin receptor with a recombinant vaccinia virus. Biochemical evidence that the insulin receptor has intrinsic serine kinase activity

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14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner

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Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins

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Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and function

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The mouse 14-3-3 epsilon isoform, a kinase regulator whose expression pattern is modulated in mesenchyme and neuronal differentiation

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IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha- and obesity-induced insulin resistance

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10.1074/JBC.272.17.11663

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