(Q28302094)

Coordinate activation of c-Src by SH3- and SH2-binding sites on a novel p130Cas-related protein, Sin.

GOA release 2020-03-11

author name string

Y Yamanashi

series ordinal

1

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D Baltimore

series ordinal

2

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language of work or name

English

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publication date

24 January 1997

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published in

Cell

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volume

88

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issue

2

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page(s)

205-11

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cites work

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Transformation by pp60src or stimulation of cells with epidermal growth factor induces the stable association of tyrosine-phosphorylated cellular proteins with GTPase-activating protein

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Functional Role of GTPase-Activating Protein in Cell Transformation by pp6Ov-src

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Src homology 2 domain as a specificity determinant in the c-Abl-mediated tyrosine phosphorylation of the RNA polymerase II carboxyl-terminal repeated domain

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

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Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases

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A target for Src in mitosis.

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Vascular endothelial cell growth factor promotes tyrosine phosphorylation of mediators of signal transduction that contain SH2 domains. Association with endothelial cell proliferation.

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Peptide-surface association: the case of PDZ and PTB domains

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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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Vascular system defects and neuronal apoptosis in mice lacking ras GTPase-activating protein

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A Grb2-associated docking protein in EGF- and insulin-receptor signalling

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The common src homology region 2 domain of cytoplasmic signaling proteins is a positive effector of v-fps tyrosine kinase function

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Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes

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PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface

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The human p62 cDNA encodes Sam68 and not the RasGAP-associated p62 protein

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A protein that is highly related to GTPase-activating protein-associated p62 complexes with phospholipase C gamma

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Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases

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Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo

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Src homology region 2 domains direct protein-protein interactions in signal transduction

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Protein-tyrosine kinases regulate the phosphorylation, protein interactions, subcellular distribution, and activity of p21ras GTPase-activating protein

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BCR first exon sequences specifically activate the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias

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The IRS-1 signaling system

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The nonreceptor protein-tyrosine kinase CSK complexes directly with the GTPase-activating protein-associated p62 protein in cells expressing v-Src or activated c-Src

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Ras complements the carboxyl terminus of v-Abl protein in lymphoid transformation.

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Getting down to specifics

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v-abl causes hematopoietic disease distinct from that caused by bcr-abl

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Negative regulation of p120GAP GTPase promoting activity by p210bcr/abl: implication for RAS-dependent Philadelphia chromosome positive cell growth

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Catalytic specificity of protein-tyrosine kinases is critical for selective signalling

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SH2 domains recognize specific phosphopeptide sequences

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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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Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1.

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An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis

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

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Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62

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