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CDH5 — SRC

Pathways - manually collected, often from reviews:

• OpenBEL Selventa BEL large corpus: CDH5 → SRC (increases)
  Evidence: Tyrosine phosphorylation of VE-cadherin is required for reducing cell–cell adhesions and is mediated through cSrc which is dependent on ROS (69, 103).

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

Studies that report less than 10 interactions are marked with *

• IRef Hprd Interaction: SRC — CDH5 (in vitro) Potter et al., J Biol Chem 2005*
• IRef Intact Interaction: SRC — CDH5 (association, pull down) Wallez et al., Oncogene 2007*

Text-mined interactions from Literome

Lin et al., Mol Pharmacol 2003 : Inhibition of vascular endothelial growth factor induced angiogenesis by resveratrol through interruption of Src dependent vascular endothelial cadherin tyrosine phosphorylation
Weis et al., J Clin Invest 2004 (Edema...) : Src blockade stabilizes a Flk/cadherin complex, reducing edema and tissue injury following myocardial infarction
Lambeng et al., Circ Res 2005 : In this model, Src inhibition impaired VEGF induced VE-cadherin phosphorylation, indicating that VE-cadherin phosphorylation was dependent on Src activation
Wallez et al., Oncogene 2007 : Finally, we found that in a VEGF induced wound healing assay, cadherin adhesive activity was impaired by Src kinase inhibitors
McLachlan et al., Mol Biol Cell 2007 : Finally, our data implicate PI3-kinase signaling as a target for cadherin activated c-Src signaling that contributes to its positive impact on cadherin function
Adam et al., J Biol Chem 2010 : Src induced tyrosine phosphorylation of VE-cadherin is not sufficient to decrease barrier function of endothelial monolayers ... In contrast, expression of constitutively active Src decreased barrier function and promoted VE-cadherin phosphorylation on tyrosines 658 and 731, although the increase in VE-cadherin phosphorylation preceded the increase in permeability by 4-6 h. Csk knockdown induced VE-cadherin phosphorylation at sites 658 and 731 but did not induce a loss in barrier function ... Taken together, our data show that Src induced tyrosine phosphorylation of VE-cadherin is not sufficient to promote an increase in endothelial cell monolayer permeability and suggest that signaling leading to changes in vascular permeability in response to inflammatory mediators or growth factors may require VE-cadherin tyrosine phosphorylation concurrently with other signaling pathways to promote loss of barrier function
Jin et al., Blood 2010 : Activated PKA blocks pp60Src dependent vascular endot helial-cadherin phosphorylation, thereby stimulating cell-cell adhesion while suppressing endothelial cell polarization, motility, angiogenesis, and vascular permeability
McLachlan et al., Cytoskeleton (Hoboken, N.J.) 2011 : Additionally, vanadate treatment phenocopied the effects of Src inhibition on the actin cytoskeleton, suggesting that PTP activity is required for the dynamic regulation of the actin cytoskeleton by cadherin activated Src signaling
Starosta et al., Am J Respir Cell Mol Biol 2012 : These data suggest that the rapid tyrosine phosphorylation of VE-cadherin and other potential targets mediated by Src and ROS dependent mechanisms plays a key role in the dissociation of AJ complexes and EC barrier dysfunction induced by high OxPAPC doses
Alcaide et al., Am J Physiol Cell Physiol 2012 : p120-Catenin prevents neutrophil transmigration independently of RhoA inhibition by impairing Src dependent VE-cadherin phosphorylation
Cho et al., Mol Biol Cell 2013 (Atherosclerosis) : Apo(a) caused the disruption of VE-cadherin/ß-catenin complexes in a Src dependent manner, decreased ß-catenin phosphorylation, and increased phosphorylation of Akt and glycogen synthase kinase-3ß, ultimately resulting in increased nuclear translocation of ß-catenin ; all of these effects are downstream of apo(a) attenuation of phosphatase and tensin homologue deleted on chromosome 10 activity
Yan et al., Stroke 2013 (Subarachnoid Hemorrhage) : Downstream to PAR-1, c-Src dependent activation of p21 activated kinase-1 led to an increased serine/threonine phosphorylation of vascular endothelial-cadherin ; immunoprecipitation results revealed an enhanced binding of phosphorylated vascular endothelial-cadherin with endocytosis orchestrator ß-arrestin-2