CrkL mediates Ras-dependent activation of the Raf/ERK pathway through the guanine nucleotide exchange factor C3G in hematopoietic cells stimulated with erythropoietin or interleukin-3. (Q30175335)

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English	CrkL mediates Ras-dependent activation of the Raf/ERK pathway through the guanine nucleotide exchange factor C3G in hematopoietic cells stimulated with erythropoietin or interleukin-3.	scientific article

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scholarly article

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Europe PubMed Central

9 June 2017

CrkL mediates Ras-dependent activation of the Raf/ERK pathway through the guanine nucleotide exchange factor C3G in hematopoietic cells stimulated with erythropoietin or interleukin-3. (English)

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Europe PubMed Central

9 June 2017

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Nosaka Y

1

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Europe PubMed Central

9 June 2017

Arai A

2

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Europe PubMed Central

9 June 2017

Miyasaka N

3

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Europe PubMed Central

9 June 2017

Miura O

4

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Europe PubMed Central

9 June 2017

language of work or name

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publication date

1 October 1999

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Europe PubMed Central

9 June 2017

Journal of Biological Chemistry

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Europe PubMed Central

9 June 2017

274

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Europe PubMed Central

9 June 2017

42

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Europe PubMed Central

9 June 2017

30154-30162

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Europe PubMed Central

9 June 2017

Cytokine receptor signalling

1 reference

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An epidermal growth factor receptor/Jak2 tyrosine kinase domain chimera induces tyrosine phosphorylation of Stat5 and transduces a growth signal in hematopoietic cells

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Signal-transducing protein phosphorylation cascades mediated by Ras/Rho proteins in the mammalian cell: the potential for multiplex signalling

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The regulation of AP-1 activity by mitogen-activated protein kinases

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A novel viral oncogene with structural similarity to phospholipase C

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Two species of human CRK cDNA encode proteins with distinct biological activities

1 reference

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C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins

1 reference

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Tyrosine 207 in CRKL is the BCR/ABL phosphorylation site

1 reference

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Erythropoietin and IL-3 induce tyrosine phosphorylation of CrkL and its association with Shc, SHP-2, and Cbl in hematopoietic cells

1 reference

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Steel factor induces tyrosine phosphorylation of CRKL and binding of CRKL to a complex containing c-kit, phosphatidylinositol 3-kinase, and p120(CBL)

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Interleukin-2 stimulation induces tyrosine phosphorylation of p120-Cbl and CrkL and formation of multimolecular signaling complexes in T lymphocytes and natural killer cells

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The CRKL adaptor protein transforms fibroblasts and functions in transformation by the BCR-ABL oncogene

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Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like growth factor-I receptor-mediated signal transduction

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Structural requirements for function of the Crkl adapter protein in fibroblasts and hematopoietic cells

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Inactivation of erythropoietin receptor function by point mutations in a region having homology with other cytokine receptors

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Reconstituted human granulocyte-macrophage colony-stimulating factor receptor transduces growth-promoting signals in mouse NIH 3T3 cells: comparison with signalling in BA/F3 pro-B cells

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Integrin activation by R-ras.

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Genetic analysis of the Kirsten-ras-revertant 1 gene: potentiation of its tumor suppressor activity by specific point mutations

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Minimal Ras-binding domain of Raf1 can be used as an activation-specific probe for Ras.

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Ras-dependent activation of c-Jun N-terminal kinase/stress-activated protein kinase in response to interleukin-3 stimulation in hematopoietic BaF3 cells

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Tyrosine 763 of the murine granulocyte colony-stimulating factor receptor mediates Ras-dependent activation of the JNK/SAPK mitogen-activated protein kinase pathway

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B cell antigen receptor signaling induces the formation of complexes containing the Crk adapter proteins

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Sos, Vav, and C3G participate in B cell receptor-induced signaling pathways and differentially associate with Shc-Grb2, Crk, and Crk-L adaptors

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CrkII signals from epidermal growth factor receptor to Ras

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Crk protein binds to PDGF receptor and insulin receptor substrate-1 with different modulating effects on PDGF- and insulin-dependent signaling pathways

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CRK protein binds to two guanine nucleotide-releasing proteins for the Ras family and modulates nerve growth factor-induced activation of Ras in PC12 cells

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v-Crk modulation of growth factor-induced PC12 cell differentiation involves the Src homology 2 domain of v-Crk and sustained activation of the Ras/mitogen-activated protein kinase pathway

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Activation of R-Ras by Ras-guanine nucleotide-releasing factor

1 reference

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Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G

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Activation of the Drosophila C3G leads to cell fate changes and overproliferation during development, mediated by the RAS-MAPK pathway and RAP1.

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A ras-related gene with transformation suppressor activity

1 reference

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cAMP activates MAP kinase and Elk-1 through a B-Raf- and Rap1-dependent pathway

1 reference

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Rap1 mediates sustained MAP kinase activation induced by nerve growth factor

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Biochemical characterization of C3G: an exchange factor that discriminates between Rap1 and Rap2 and is not inhibited by Rap1A(S17N).

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Extracellular signal-regulated activation of Rap1 fails to interfere in Ras effector signalling

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Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation

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Involvement of prolonged ras activation in thrombopoietin-induced megakaryocytic differentiation of a human factor-dependent hematopoietic cell line

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Downstream of Crk adaptor signaling pathway: activation of Jun kinase by v-Crk through the guanine nucleotide exchange protein C3G.

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Guanine-nucleotide exchange protein C3G activates JNK1 by a ras-independent mechanism. JNK1 activation inhibited by kinase negative forms of MLK3 and DLK mixed lineage kinases

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Activation of Rac1 by a Crk SH3-binding protein, DOCK180

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The adaptor protein Crk connects multiple cellular stimuli to the JNK signaling pathway

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DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane

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Suppression of integrin activation: a novel function of a Ras/Raf-initiated MAP kinase pathway

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Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G

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10.1074/JBC.274.42.30154

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Europe PubMed Central

9 June 2017

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