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TM, especially TME45, maintains vascular integrity, at least in part, via Src signaling.
We conclude that pp60(Src) can directly inhibit DDAH (show DDAH2 Proteins) II and this is involved in the increased ADMA levels that enhance eNOS (show NOS3 Proteins) uncoupling during the development of acute lung injury (ALI).
Ambra1 (show AMBRA1 Proteins) binds to both FAK (show PTK2 Proteins) and Src in cancer cells. When FAK (show PTK2 Proteins) is present, Ambra1 (show AMBRA1 Proteins) is recruited to focal adhesions, promoting FAK (show PTK2 Proteins)-regulated cancer cell direction-sensing and invasion. However, when Ambra1 (show AMBRA1 Proteins) cannot bind to FAK (show PTK2 Proteins), abnormally high levels of phospho-Src and phospho-FAK (show PTK2 Proteins) accumulate at focal adhesions, positively regulating adhesion and invasive migration.
Thus we propose that Cx43 (show GJA1 Proteins) might enhance the activation of Nrf2 (show NFE2L2 Proteins)/ARE pathway by means of inhibiting c-Src activity to hinder the nuclear export of Nrf2 (show NFE2L2 Proteins), and then reduce expression of FN, ICAM-1 (show ICAM1 Proteins) and TGF-b1, ultimately attenuating renal fibrosis in diabetes.
Osteoprotegerin (show TNFRSF11B Proteins) may induce podosome reassembly and peripheral adhesive structure detachment by modulating phosphorylation of Pyk2 (show PTK2B Proteins) and Src and their intracellular distribution in osteoclasts.
BMP2 (show BMP2 Proteins) also requires Src for filamentous actin polymerization in Tgfbr3 (show TGFBR3 Proteins)(-/-) epicardial cells.
v-Src prevents nuclear exclusion of YAP (show YAP1 Proteins) through a decrease in the phosphorylation of YAP (show YAP1 Proteins) at Ser127 in multinucleated cells.
These results revealed that vascular sprouting and permeability are both controlled through the VEGFR2-TSAd-c-Src signaling pathway in a subset of tissues, which may be useful in developing strategies to control tissue-specific pathological angiogenesis.
The TBK1 (show TBK1 Proteins) Y179A mutant failed to rescue type I IFN production by virally infected RAW264.7 macrophages deficient in TBK1 (show TBK1 Proteins).
identified both Syk (show SYK Proteins) and Src signaling pathways as ones that participate in Borrelia burgdorferi phagocytosis and the resulting cytokine activation.
Src64 controls actin dynamics to mediate proper ring canal formation during incomplete cytokinesis during germline cyst development in vivo
that Brat represses the translation of src64B, an upstream regulator of a conserved Rho-dependent pathway previously shown to promote axon retraction
Results show that Src42a and Src64b are required for the normal division capacity of Drosophila intestinal progenitor cells, and that these genes as well as Ack cause progenitor overproliferation in the intestine via core cell cycle activation.
a novel essential role for Src in intestinal stem/progenitor cell proliferation and tumourigenesis initiation in vivo.
Data show that the actin-Capping Protein (show TMOD4 Proteins) (CP) alphabeta heterodimer, which regulates actin (show ACTB Proteins) filament (F-actin (show ACTB Proteins)) polymerization, limits Src-induced apoptosis or tissue overgrowth by restricting JNK (show MAPK8 Proteins) activation.
Dumbfounded/Neph1 (show NEPH1 Proteins), a key diaphragm constituent, is a target of the Src kinase (show CSK Proteins) Src64B. Loss of Src64B activity leads to a reduction in the number of diaphragms, and this effect is in part mediated by loss of Dumbfounded/Neph1 (show NEPH1 Proteins) tyrosine phosphorylation.
Homodimerization of the Wnt receptor DERAILED recruits the Src family kinase SRC64B in the developing embryonic central nervous system.
E4orf4 has a role in inducing PP2A (show PPP2R2B Proteins)- and Src-dependent cell death while inhibiting classic apoptosis pathways in Drosophila melanogaster
Mutations in a Drosophila src gene, src64, that alter the three HRD amino acids, were identified.
Src64B overexpression induced the formation of specialized haemocytes (lamellocytes), but had no effect on circulating plasmatocyte concentration. Src64B overexpression induced F-actin (show ACTB Proteins) formation and Jun kinase (show MAPK9 Proteins) activation in plasmatocytes.
Findings indicate the importance of Src-Stat3 (show STAT3 Proteins) signaling cascade in gallic acid (GA)-mediated tumor-suppression activity and a therapeutic insight of GA for acquired resistance to EGF receptor (show EGFR Proteins) tyrosine kinase (show RET Proteins) inhibitors in lung cancer.
Memo (show MEMO1 Proteins) facilitates ER-alpha (show ESR1 Proteins) and c-Src interaction, ER-alpha (show ESR1 Proteins) Y537 phosphorylation, and has the ability to control ER-alpha (show ESR1 Proteins) extra-nuclear localization in breast cancer cells.
Data show that MLLT11/AF1q (show MLLT11 Proteins)-induced PDGFR (show PDGFRB Proteins) signaling enhanced STAT3 (show STAT3 Proteins) activity through Src kinase (show CSK Proteins) activation.
Loss of myristoylation abolished the tumorigenic potential of Src and its synergy with androgen receptor (show AR Proteins) in mediating tumor invasion.
N-WASP positively regulates demarcation membrane system development and proplatelet formation, and the Src family kinases in association with CDC42 regulate proplatelet formation through N-WASP
phosphorylation of mATG9 (show ATG9A Proteins) at Tyr8 by Src and at Ser14 by ULK1 (show ULK1 Proteins) functionally cooperate to promote interactions between mATG9 (show ATG9A Proteins) and the AP1 (show FOSB Proteins)/2 complex.
Data suggest that myristoylation of Src kinase (show CSK Proteins) is essential to facilitate Src-induced and high-fat diet-accelerated prostatic tumor progression; targeting Src kinase (show CSK Proteins) myristoylation, which is required for Src kinase (show CSK Proteins) association at cellular membrane, blocks dietary fat-accelerated tumorigenesis.
elevated levels of cellular Src in serum and phosphorylated Src in primary nasopharyngeal carcinoma tissue correlated with poor outcomes of these patients
Results indicate that src-family kinase (Src) is a upstream kinase of T-LAK cell-originated protein kinase (TOPK (show PBK Proteins)).
We suggest that the induction of SRC results in increased prostate cancer metastasis that is linked to the dysregulation of the AR signaling pathway through the inactivation of miR (show MLXIP Proteins)-203
RhoA (show RHOA Proteins) and membrane fluidity mediates the spatially polarized Src/FAK (show PTK2 Proteins) activation in response to shear stress.
AngII activates PKD via a mechanism involving Src family kinases and PKC, to underlie increased aldosterone production.
The Src gene possibly contributed to conducting association analysis and can be recognized as genetic marker in milk production traits and other performance for animal breeding and genetics.
src has a role in activation of 5'-AMP (show TMPRSS5 Proteins)-activated kinase during hypoxia-reoxygenation of bovine aortic endothelial cells
results indicate that integrin engagement disrupts VE-cadherin-containing adherens junctions via the activation of Src, but not Ras, possibly as a result of modulation of the actin network
These results suggest that TGF-beta1 (show TGFB1 Proteins)-induced monolayer permeability involves focal adhesion and cytoskeletal rearrangement through both FAK (show PTK2 Proteins)/Src-dependent and -independent pathways.
The findings are consistent with previous studies that indicate a link between Na,K-ATPase (show ATP1A1 Proteins) activity and SFK signaling.
Src kinase (show CSK Proteins) mediates hypoxia-induced caspase-1 (show CASP1 Proteins) activation in the cerebral cortex of newborn piglets
Expression of mutant alpha1 Na/K-ATPase (show ATP1A1 Proteins) defective in conformational transition attenuates Src-mediated signal transduction
20-HETE activates the Raf/MEK/ERK pathway in renal epithelial cells through an EGFR- and c-Src-dependent mechanism.
This gene is highly similar to the v-src gene of Rous sarcoma virus. This proto-oncogene may play a role in the regulation of embryonic development and cell growth. The protein encoded by this gene is a tyrosine-protein kinase whose activity can be inhibited by phosphorylation by c-SRC kinase. Mutations in this gene could be involved in the malignant progression of colon cancer. Two transcript variants encoding the same protein have been found for this gene.
proto-oncogene tyrosine-protein kinase SRC
, proto-oncogene tyrosine-protein kinase src
, neuronal proto-oncogene tyrosine-protein kinase Src
, proto-oncogene c-Src
, Src proto oncogene sequence
, mRNA-like ncRNA in embryogenesis 5
, proto-oncogene tyrosine-protein kinase Src
, protooncogene SRC, Rous sarcoma
, tyrosine kinase pp60c-src
, tyrosine-protein kinase SRC-1
, Rous sarcoma oncogene
, tyrosine protein kinase c-src
, tyrosine protein kinase pp60-c-src
, v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog
, src oncogene
, v-src avian sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog
, non-tyrosine protein kinase