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CTNNB1 — SRC
Pathways - manually collected, often from reviews:
-
OpenBEL Selventa BEL large corpus:
CTNNB1
→
SRC
(increases, CTNNB1 Activity)
Evidence: The rates of oxidative stress-induced activation of c-Src, tyrosine phosphorylation of ZO-1 and beta-catenin, decrease in resistance, increase in permeability to inulin, and redistribution of occludin and ZO-1 were significantly greater in cells transfected with wild type c-Src, whereas it was low in cells transfected with kinase-inactive c-SrcK297R mutant, when compared with those in empty vector-transfected cells.
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KEGG Adherens junction:
SRC
→
CTNNB1
(protein-protein, inhibition)
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NCI Pathway Database Posttranslational regulation of adherens junction stability and dissassembly:
Src (SRC)
→
E-cadherin/beta catenin/alpha catenin complex (CDH1-CTNNB1-CTNNA1)
(modification, activates)
Fujita et al., Nat Cell Biol 2002, Palacios et al., Mol Cell Biol 2005
Evidence: mutant phenotype, assay, other species
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NCI Pathway Database Posttranslational regulation of adherens junction stability and dissassembly:
Src (SRC)
→
E-cadherin/beta catenin complex (CDH1-CTNNB1)
(modification, activates)
Fujita et al., Nat Cell Biol 2002, Palacios et al., Mol Cell Biol 2005
Evidence: mutant phenotype, assay, other species
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NCI Pathway Database Signaling events mediated by Hepatocyte Growth Factor Receptor (c-Met):
E-cadherin/beta catenin/alpha cateninNUMB/Par3/Par6/Atypical PKCs complex (CDH1-NUMB-CTNNB1-CTNNA1-F2RL2-PARD6A-PRKCI_PRKCZ)
→
Src (SRC)
(modification, collaborate)
Wang et al., EMBO J 2009
Evidence: physical interaction
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NCI Pathway Database Posttranslational regulation of adherens junction stability and dissassembly:
Src (SRC)
→
E-cadherin/Ca2+/beta catenin/alpha catenin/p120 catenin complex (CDH1-CTNNB1-CTNNA1-CTNND1)
(modification, activates)
Roura et al., J Biol Chem 1999, Piedra et al., J Biol Chem 2001, Fujita et al., Nat Cell Biol 2002, Duchesne et al., J Biol Chem 2003, Simoneau et al., Cell Signal 2011
Evidence: assay, physical interaction
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NCI Pathway Database E-cadherin signaling in keratinocytes:
E-cadherin/beta catenin-gamma catenin complex (CDH1-CTNNB1_JUP)
→
Src (SRC)
(modification, collaborate)
Xie et al., Mol Biol Cell 2005, Calautti et al., J Cell Biol 1998
Evidence: assay, physical interaction, other species
-
NCI Pathway Database E-cadherin signaling in keratinocytes:
Src (SRC)
→
E-cadherin/beta catenin-gamma catenin/alpha catenin/p120 catenin complex (CDH1-CTNNB1_JUP-CTNNA1-CTNND1)
(modification, activates)
Xie et al., Mol Biol Cell 2005, Calautti et al., J Cell Biol 1998
Evidence: assay, physical interaction, other species
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
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MIPS CORUM Polycystin-1 multiprotein complex (ACTN1, CDH1, SRC, JUP, VCL, CTNNB1, PXN, BCAR1, PKD1, PTK2, TLN1):
Polycystin-1 multiprotein complex (ACTN1, CDH1, SRC, JUP, VCL, CTNNB1, PXN, BCAR1, PKD1, PTK2, TLN1) complex (ACTN1-BCAR1-CDH1-CTNNB1-JUP-PKD1-PTK2-PXN-SRC-TLN1-VCL)
Geng et al., Biochim Biophys Acta 2000
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IRef Corum Interaction:
Complex of 12 proteins
(association, cosedimentation through density gradient)
Geng et al., Biochim Biophys Acta 2000
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IRef Dip Interaction:
SRC
—
CTNNB1
(direct interaction, protein kinase assay)
Yang et al., Nature 2011*
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IRef Dip Interaction:
SRC
—
CTNNB1
(direct interaction, anti bait coimmunoprecipitation)
Yang et al., Nature 2011*
-
IRef Hprd Interaction:
SRC
—
CTNNB1
(in vitro)
Piedra et al., J Biol Chem 2001
Text-mined interactions from Literome
Li et al., J Biol Chem 2001
:
The findings support a novel
role for
c-Src in regulating interactions of MUC1 with GSK3 beta and
beta-catenin
Farkas et al., J Neurosci Res 2005
:
Hyperosmotic mannitol induces
Src kinase
dependent phosphorylation of
beta-catenin in cerebral endothelial cells
Karni et al., Mol Cell Biol 2005
:
Activated
Src enhances the accumulation of nuclear
beta-catenin and enhances its transcriptional activity, elevating target genes such as cyclin D1
Coluccia et al., Cancer Res 2006
(Colorectal Neoplasms) :
SKI-606 decreases growth and motility of colorectal cancer cells by preventing
pp60(c-Src) dependent tyrosine phosphorylation of
beta-catenin and its nuclear signaling ...
Src dependent
activation of
beta-catenin was prevented by SKI-606, a novel Src family kinase inhibitor, which also abrogated beta-catenin nuclear function by impairing its binding to the TCF4 transcription factor and its trans activating ability in colorectal cancer cells
Chen et al., Cancer Lett 2008
:
An acidic extracellular pH induces
Src kinase
dependent loss of
beta-catenin from the adherens junction ... The acidic pHe induced
c-Src activation
increased tyrosine phosphorylation of
beta-catenin and decreased the amount of beta-catenin associated E-cadherin
Inge et al., Mol Cancer Ther 2008
:
alpha-Catenin overrides
Src dependent activation of
beta-catenin oncogenic signaling ... Further,
Src mediated tyrosine phosphorylation of
beta-catenin is a major mechanism for decreased beta-catenin interaction with E-cadherin in alpha-catenin-null cells
Chang et al., Oncogene 2008
(Prostatic Neoplasms) :
Src inhibition
resulted in decreased binding of
beta-catenin to the promoters of G1 phase cell cycle regulators cyclin D1 and c-Myc
Desprat et al., Dev Cell 2008
:
We find that stomodeal compression triggers
Src42A dependent nuclear translocation of
Armadillo/beta-catenin , which is required for Twist mechanical induction in the stomodeum
Chen et al., J Cell Biochem 2009
:
We have previously shown that culturing HepG2 cells in pH 6.6 culture medium increases the
c-Src dependent tyrosine phosphorylation of
beta-catenin and induces disassembly of adherens junctions ( AJs )
Zhang et al., Blood 2009
(MAP Kinase Signaling System) :
Src can directly interact with beta-catenin and
trigger nuclear translocation of
beta-catenin