Tyrosine phosphorylation of C-Cbl facilitates adhesion and spreading while suppressing anchorage-independent growth of V-Abl-transformed NIH3T3 fibroblasts (Q40944647)

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scientific article published on June 1999

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English	Tyrosine phosphorylation of C-Cbl facilitates adhesion and spreading while suppressing anchorage-independent growth of V-Abl-transformed NIH3T3 fibroblasts	scientific article published on June 1999

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scholarly article

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Europe PubMed Central

PubMed publication ID

25 September 2017

Tyrosine phosphorylation of C-Cbl facilitates adhesion and spreading while suppressing anchorage-independent growth of V-Abl-transformed NIH3T3 fibroblasts (English)

1 reference

Europe PubMed Central

PubMed publication ID

25 September 2017

phosphorylation

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E A Feshchenko

1

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Europe PubMed Central

PubMed publication ID

25 September 2017

S K Shore

2

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Europe PubMed Central

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25 September 2017

A Y Tsygankov

3

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Europe PubMed Central

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25 September 2017

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publication date

1 June 1999

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Europe PubMed Central

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25 September 2017

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Europe PubMed Central

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25 September 2017

18

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Europe PubMed Central

PubMed publication ID

25 September 2017

25

1 reference

Europe PubMed Central

PubMed publication ID

25 September 2017

3703-3715

1 reference

Europe PubMed Central

PubMed publication ID

25 September 2017

Activation of Rho-dependent cell spreading and focal adhesion biogenesis by the v-Crk adaptor protein

1 reference

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Phosphorylation of Cbl following stimulation with interleukin-3 and its association with Grb2, Fyn, and phosphatidylinositol 3-kinase

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Interactions of Cbl with two adapter proteins, Grb2 and Crk, upon T cell activation

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The protein product of the c-cbl protooncogene is phosphorylated after B cell receptor stimulation and binds the SH3 domain of Bruton's tyrosine kinase

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Crkl is complexed with tyrosine-phosphorylated Cbl in Ph-positive leukemia

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Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases

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The lipid products of phosphoinositide 3-kinase increase cell motility through protein kinase C.

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Fyn, Yes, and Syk phosphorylation sites in c-Cbl map to the same tyrosine residues that become phosphorylated in activated T cells

1 reference

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Association of tyrosine protein kinase Zap-70 with the protooncogene product p120c-cbl in T lymphocytes

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Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate

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T cell activation-dependent association between the p85 subunit of the phosphatidylinositol 3-kinase and Grb2/phospholipase C-gamma 1-binding phosphotyrosyl protein pp36/38.

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Signaling through focal adhesion kinase

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Formation of c-Cbl.phosphatidylinositol 3-kinase complexes on lymphocyte membranes by a p56lck-independent mechanism

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Specific association of the beta isoform of the p85 subunit of phosphatidylinositol-3 kinase with the proto-oncogene c-cbl

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

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Cdc42 and Rac1 induce integrin-mediated cell motility and invasiveness through PI(3)K.

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Ras-dependent, Ca2+-stimulated activation of nuclear factor of activated T cells by a constitutively active Cbl mutant in T cells.

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A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T cells

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Interactions of Cbl with Grb2 and phosphatidylinositol 3'-kinase in activated Jurkat cells

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Coupling of the Proto-oncogene Product c-Cbl to the Epidermal Growth Factor Receptor

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A beta 1 integrin signaling pathway involving Src-family kinases, Cbl and PI-3 kinase is required for macrophage spreading and migration

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The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor alpha

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The proto-oncogene product c-Cbl becomes tyrosine phosphorylated by stimulation with GM-CSF or Epo and constitutively binds to the SH3 domain of Grb2/Ash in human hematopoietic cells

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Oncogenic forms of Cbl abrogate the anchorage requirement but not the growth factor requirement for proliferation

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The proto-oncogene product p120(cbl) links c-Src and phosphatidylinositol 3'-kinase to the integrin signaling pathway.

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p120cbl is a major substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and Shc adaptors, and the p85 subunit of phosphatidylinositol 3-kinase

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10.1038/SJ.ONC.1202672

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Europe PubMed Central

PubMed publication ID

25 September 2017

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PubMed publication ID

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Europe PubMed Central

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25 September 2017

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