Distinct modes of interaction of SHC and insulin receptor substrate-1 with the insulin receptor NPEY region via non-SH2 domains (Q24310517)

GOA release 2020-03-11

insulin receptor

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insulin receptor signaling pathway

GOA release 2020-03-11

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Journal of Biological Chemistry

GOA release 2020-03-11

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3

T A Gustafson

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author name string

W He

series ordinal

1

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T J O'Neill

series ordinal

2

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language of work or name

English

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publication date

6 October 1995

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published in

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volume

270

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issue

40

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page(s)

23258-62

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cites work

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

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Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1

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YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase

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A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction

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

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An alternative to SH2 domains for binding tyrosine-phosphorylated proteins

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A phosphotyrosine interaction domain

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Transformation by polyoma virus middle T-antigen involves the binding and tyrosine phosphorylation of Shc.

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Polyoma middle tumor antigen interacts with SHC protein via the NPTY (Asn-Pro-Thr-Tyr) motif in middle tumor antigen.

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Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF responses

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A conserved amino-terminal Shc domain binds to phosphotyrosine motifs in activated receptors and phosphopeptides

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Common elements in interleukin 4 and insulin signaling pathways in factor-dependent hematopoietic cells.

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

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Fused protein domains inhibit DNA binding by LexA

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

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

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

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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Shc Binding to Nerve Growth Factor Receptor Is Mediated by the Phosphotyrosine Interaction Domain

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The phosphotyrosine interaction domain of Shc binds an LXNPXY motif on the epidermal growth factor receptor

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PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine

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The phosphotyrosine interaction domain of SHC recognizes tyrosine-phosphorylated NPXY motif

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Insulin rapidly stimulates tyrosine phosphorylation of a Mr-185,000 protein in intact cells

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High-efficiency transformation of yeast by electroporation

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7 January 2021

The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation

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An IL-4 receptor region containing an insulin receptor motif is important for IL-4-mediated IRS-1 phosphorylation and cell growth

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7 January 2021

The insulin receptor and its substrate: molecular determinants of early events in insulin action.

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7 January 2021