Identification of SNT/FRS2 docking site on RET receptor tyrosine kinase and its role for signal transduction (Q28189821)

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T Iwashita

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H Murakami

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H Hayashi

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K Kawai

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M Takahashi

GDNF family neurotrophic factor signaling: four masters, one servant?

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language of work or name

English

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publication date

12 April 2001

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1929-38

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cites work

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Identification of Shc docking site on Ret tyrosine kinase

21 January 2018

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A mutation at tyrosine 1062 in MEN2A-Ret and MEN2B-Ret impairs their transforming activity and association with shc adaptor proteins

21 January 2018

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Signaling complexes and protein-protein interactions involved in the activation of the Ras and phosphatidylinositol 3-kinase pathways by the c-Ret receptor tyrosine kinase.

21 January 2018

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Signaling through Ras is essential for ret oncogene-induced cell differentiation in PC12 cells.

21 January 2018

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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

21 January 2018

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Shc and Enigma are both required for mitogenic signaling by Ret/ptc2.

21 January 2018

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Two distinct mutations of the RET receptor causing Hirschsprung's disease impair the binding of signalling effectors to a multifunctional docking site

21 January 2018

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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

21 January 2018

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Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation

21 January 2018

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Characterization of intracellular signals via tyrosine 1062 in RET activated by glial cell line-derived neurotrophic factor

21 January 2018

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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

21 January 2018

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The role of amino acids surrounding tyrosine 1062 in ret in specific binding of the shc phosphotyrosine-binding domain

21 January 2018

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A two-hit model for development of multiple endocrine neoplasia type 2B by RET mutations

21 January 2018

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A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway

21 January 2018

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The signaling adapter FRS-2 competes with Shc for binding to the nerve growth factor receptor TrkA. A model for discriminating proliferation and differentiation

21 January 2018

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Rho-dependent and -independent tyrosine phosphorylation of focal adhesion kinase, paxillin and p130Cas mediated by Ret kinase

21 January 2018

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Enhanced phosphatidylinositol 3-kinase activity and high phosphorylation state of its downstream signalling molecules mediated by ret with the MEN 2B mutation

21 January 2018

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Characterization of Ret-Shc-Grb2 complex induced by GDNF, MEN 2A, and MEN 2B mutations

21 January 2018

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FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors

21 January 2018

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Transforming ability of MEN2A-RET requires activation of the phosphatidylinositol 3-kinase/AKT signaling pathway.

21 January 2018

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SNT, a Differentiation-Specific Target of Neurotrophic Factor-Induced Tyrosine Kinase Activity in Neurons and PC12 Cells

21 January 2018

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A role for the SHP-2 tyrosine phosphatase in nerve growth-induced PC12 cell differentiation

21 January 2018

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Novel recognition motif on fibroblast growth factor receptor mediates direct association and activation of SNT adapter proteins

21 January 2018

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Biological and biochemical properties of Ret with kinase domain mutations identified in multiple endocrine neoplasia type 2B and familial medullary thyroid carcinoma

21 January 2018

1 reference

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inferred from DOI database lookup

7 January 2021

based on heuristic

RET alternate splicing influences the interaction of activated RET with the SH2 and PTB domains of Shc, and the SH2 domain of Grb2

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1204290