Sprouty proteins are in vivo targets of Corkscrew/SHP-2 tyrosine phosphatases (original) (raw)

Phosphorylation of Carboxyl-terminal Tyrosines Modulates the Specificity of Sprouty-2 Inhibition of Different Signaling Pathways

Dina Ron

Journal of Biological Chemistry, 2005

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Tyrosine Phosphorylation of Sprouty Proteins Regulates Their Ability to Inhibit Growth Factor Signaling: A Dual Feedback Loop

Hamid Band

Molecular Biology of the Cell, 2004

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The Nonreceptor Protein Tyrosine Phosphatase Corkscrew Functions in Multiple Receptor Tyrosine Kinase Pathways inDrosophila

Norbert Perrimon

Developmental Biology, 1996

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Tyrosine Phosphorylation of Sprouty2 Enhances Its Interaction with c-Cbl and Is Crucial for Its Function

Graeme Guy

Journal of Biological Chemistry, 2003

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Mammalian Sprouty Proteins Inhibit Cell Growth and Differentiation by Preventing Ras Activation

Miriam Benezra

Journal of Biological Chemistry, 2001

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Intermolecular Interactions of Sprouty Proteins and Their Implications in Development and Disease

Francis Edwin

Molecular Pharmacology, 2009

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Graeme Guy

The Journal of biological chemistry, 2011

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Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling

Graeme Guy

The EMBO Journal, 2002

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Sprouty proteins: modified modulators, matchmakers or missing links?

Graeme Guy

Journal of Endocrinology, 2009

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Sprouty2 Interacts with Protein Kinase Cδ and Disrupts Phosphorylation of Protein Kinase D1

Graeme Guy

The Journal of Biological Chemistry, 2009

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Sprouty proteins are targeted to membrane ruffles upon growth factor receptor tyrosine kinase activation. Identification of a novel translocation domain

Graeme Guy

The Journal of biological chemistry, 2000

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Direct association of Sprouty-related protein with an EVH1 domain (SPRED) 1 or SPRED2 with DYRK1A modifies substrate/kinase interactions

Graeme Guy

The Journal of biological chemistry, 2010

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Distinct requirements for the Sprouty domain for functional activity of Spred proteins

Peter Lock

Biochemical Journal, 2005

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Phosphatidylinositol Phosphate Kinase Type Iγ Directly Associates with and Regulates Shp-1 Tyrosine Phosphatase

Maria Brito Diaz

Journal of Biological Chemistry, 2005

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Mammalian Sprouty-1 and -2 Are Membrane-Anchored Phosphoprotein Inhibitors of Growth Factor Signaling in Endothelial Cells

amelia compagni

Journal of Cell Biology, 2001

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The Receptor Tyrosine Kinase Regulator Sprouty1 Is a Target of the Tumor Suppressor WT1 and Important for Kidney Development

Patricia Wilson

Journal of Biological Chemistry, 2003

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Direct Binding of PP2A to Sprouty2 and Phosphorylation Changes Are a Prerequisite for ERK Inhibition Downstream of Fibroblast Growth Factor Receptor Stimulation

Graeme Guy

Journal of Biological Chemistry, 2007

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A Src Homology 3-binding Sequence on the C Terminus of Sprouty2 Is Necessary for Inhibition of the Ras/ERK Pathway Downstream of Fibroblast Growth Factor Receptor Stimulation

tt saw

Journal of Biological Chemistry, 2006

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A novel function for the protein tyrosine phosphatase Shp2 during lung branching morphogenesis

David Warburton

Developmental Biology, 2005

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Sprouty2 Inhibits the Ras/MAP Kinase Pathway by Inhibiting the Activation of Raf

Graeme Guy

Journal of Biological Chemistry, 2002

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Site-Specific Incorporation of a Phosphotyrosine Mimetic Reveals a Role for Tyrosine Phosphorylation of SHP-2 in Cell Signaling

Tony Hunter

Molecular Cell, 2001

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The tyrosine phosphatase SHP-2 is required for mediating phosphatidylinositol 3-kinase/Akt activation by growth factors

Mark Greene

Oncogene, 2001

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Sprouty: a common antagonist of FGF and EGF signaling pathways in Drosophila

Mark Krasnow

Development (Cambridge, England), 1999

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Spatial signal repression as an additional role of Sprouty2 protein variants

yared teshome

Cellular Signalling, 2019

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Sprouty1 Controls Genitourinary Development via its N-Terminal Tyrosine

Joan Ribera

Journal of the American Society of Nephrology, 2019

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Sprouty2 and Spred1-2 Proteins Inhibit the Activation of the ERK Pathway Elicited by Cyclopentenone Prostanoids

Jose Rojas

PLoS ONE, 2011

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Regulation of Sprouty2 stability by mammalian Seven-in-Absentia homolog 2

Dmitry Kovalenko

Journal of Cellular Biochemistry, 2007

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Tesk1 Interacts with Spry2 to Abrogate Its Inhibition of ERK Phosphorylation Downstream of Receptor Tyrosine Kinase Signaling

Graeme Guy

Journal of Biological Chemistry, 2008

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Sprouty proteins are in vivo targets of Corkscrew/SHP-2 tyrosine phosphatases (original) (raw)

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