Gene interactions and pathways from curated databases and text-mining

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CBL — SRC

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Suzuki et al., J Immunol 2000 : Tyrosine phosphorylation of Vav and c-Cbl was restored in common by a-Lyn, a-Hck, and a-Src , but Fc gamma RIIB tyrosine phosphorylation, which is implicated in negative signaling, was reconstituted solely by a-Lyn and a-Hck
Hakak et al., Oncogene 2000 : Activation of PI3-kinase by v-Src may be mediated by the association of the adapter protein Cbl with the p85 subunit
Sanjay et al., J Cell Biol 2001 : The activation of integrin alpha(v)beta ( 3 ) induces the [ Ca ( 2+ ) ] ( i ) -dependent phosphorylation of Pyk2 Y402, its association with Src SH2, Src activation , and the Src SH3 dependent recruitment and phosphorylation of c-Cbl
Magnifico et al., J Biol Chem 2003 : Cbl-b also targets active Src for degradation in cells, and Nedd4 similarly reverses Cbl mediated Src degradation
Kim et al., Oncogene 2004 (Cell Transformation, Neoplastic) : The level of v-Src protein was reduced by Cbl-c , possibly through a lysosome dependent pathway
Valverde et al., J Bone Miner Res 2005 (Bone Resorption) : c-Src dependent c-Cbl phosphorylation was 8-fold higher in RAW264.7 cells treated with BSP and RANKL than in those treated with RANKL alone
Sanjay et al., FEBS J 2006 : We previously showed that the primary interaction between Src and Cbl is mediated by the Src homology domain 3 (SH3) of Src binding to proline-rich sequences of Cbl ... Mutating Cbl prolines 543-548 to alanines substantially reduced Src binding to Cbl, Src induced phosphorylation of Cbl , and the inhibition of Src kinase activity by Cbl ... In contrast, disabling the tyrosine kinase binding domain of full-length Cbl by mutating glycine 306 to glutamic acid, and thereby preventing the previously described binding of the tyrosine kinase binding domain to the Src phosphotyrosine 416, had no effect on Cbl phosphorylation, the inhibition of Src activity by full-length Cbl, or bone resorption
Dragone et al., Proc Natl Acad Sci U S A 2006 : Src-like adaptor protein (SLAP) regulates B cell receptor levels in a c-Cbl dependent manner
Eisinger et al., J Biol Chem 2009 (MAP Kinase Signaling System) : The failure of morphine to desensitize ERK1/2 signaling is mediated by persistent activation of c-Src , which induces degradation of c-Cbl
Song et al., Cell Signal 2010 : Data from gene knockdown experiments with an RNA interference ( RNAi ) technique show that c-Cbl is involved in the interaction between Src and PI3K p85 during TRAIL treatment, playing an important role in TRAIL induced Akt phosphorylation
Samoylenko et al., Carcinogenesis 2012 (Adenocarcinoma...) : Thereby, Ruk ( l ) /CIN85 led to a more rapid and prolonged epidermal growth factor dependent activation of Src , Akt and ERK1/2 and treatment with the Src inhibitor PP2 and the PI3K inhibitor LY294002 abolished the Ruk ( l ) /CIN85 dependent changes in cell motility
Lee et al., J Biol Chem 2012 : Src inhibition blocked metformin mediated Cbl phosphorylation, suggesting that metformin stimulates AMPK-Src-Cbl axis pathway
Ryan et al., PloS one 2012 : Binding of Hic-5 to Cbl-c leads to an increase in the ubiquitin ligase activity of Cbl-c once Cbl-c has been activated by Src phosphorylation or through an activating phosphomimetic mutation
Deckert et al., J Biol Chem 1998 : These findings implicate Fyn as an adaptor protein that facilitates the interaction between Syk and Cbl, and suggest that Src and Syk family PTKs coordinately regulate the tyrosine phosphorylation of Cbl