Recombinant Mouse Tyrosine-protein kinase CSK (Csk)

1. Our results have uncovered a previously unknown role of c-Src tyrosine kinase in regulating interneuron function in the brain and identified a novel mechanism by which TASK-1 channels are activated in neurons. PMID: 28714121
2. in the absence of PAG, Csk becomes more associated with alternative partners; i.e., phosphatase PTPN22 and Dok adaptors. Combining PAG deficiency with PTPN22 or Dok adaptor deficiency further enhances effector T cell responses. Unlike PAG, Cbl ubiquitin ligases inhibit the activation of naive, but not of effector, T cells. PMID: 27926878
3. Csk is a causative gene in the 15q24 locus and regulates blood pressure through Src, and these findings provide a novel therapeutic target for the treatment of hypertension PMID: 26751575
4. Csk plays an important role, not only in basal signaling, but also in setting the T cell antigen receptor signaling threshold and affinity recognition. PMID: 26302204
5. SHIP1 and Csk are part of the PSTPIP2-dependent inhibitory network that prevents the development of autoinflammatory disease. PMID: 26304991
6. If Cbp enhances the interaction between c-Src and FAK, Cbp could promote c-Src function when lipid rafts are disrupted. PMID: 24675741
7. Differentiation of embryonic stem cells is driven by c-Src is antagonized by c-Yes. PMID: 23895624
8. critical role in preventing TCR signaling PMID: 24317039
9. It was concluded that c-Src and NADPH oxidase components are necessary for redox-mediated production of TNF-alpha following liver ischemia-reperfusion and that hepatocytes play an important role in this process. PMID: 23639811
10. Data indicate that chemical rescue of c-Src provided a tool to dissect the spatiotemporal mechanism of activation of the Rap1 guanine exchange factor, C3G, one of the identified potential c-Src substrates that plays a role in focal adhesion signaling. PMID: 22499769
11. The Csk pathway appears to be a critical signaling cascade regulating social learning and memory PMID: 22348736
12. These data demonstrate that expression of an activated allele of c-src overcomes the block to mammary gland morphogenesis in mice arising due to the loss of the cytoplasmic C-terminal domain of Ptch1. PMID: 22968113
13. Data show that the phosphoprotein associated with glycosphigolipid-enriched microdomains (PAG)/Csk binding protein (Cbp) modulates SFK activity in the brain. PMID: 21915273
14. Caveolin-1 and C-terminal Src kinase binding protein are cooperative, and increases in their expression or phosphorylation favors repression of C-terminal Src kinase activity. PMID: 21778303
15. expression of Cbp is downregulated during osteoclast differentiation, consequently inhibiting recruitment of Csk to lipid rafts and keeping c-Src activity high in osteoclasts. findings provide a novel paradigm that controls c-Src activity in osteoclasts. PMID: 19874196
16. show that relative titration of CD45 and Csk expression reveals distinct regulation of basal and inducible T cell receptor signaling during thymic development. PMID: 20346773
17. Results identify Src-family kinase substrates involved in platelet-derived growth factor signaling. PMID: 19632164
18. the absence of c-src expression indeed affects the development of selected, TCDD-induced toxic endpoints that are related to wasting syndrome PMID: 11882352
19. role for Csk in P. aeruginosa invasion, while providing further evidence that actin cytoskeleton disruption contributes to ExsA-regulated P. aeruginosa cytotoxicity and invasion inhibition PMID: 12220990
20. integrin-mediated signals in Csk-deficient fibroblasts (Csk(-) cells) and their stable transfectants expressing re-introduced Csk (Csk(-)/Csk cells) PMID: 12670507
21. the loss of IGF-I downstream mitogenic signaling in differentiating 3T3-L1 cells is due to a change in IGF-I activation of c-Src and CSK may mediate the inactivation of c-Src by IGF-I in 3T3-L1 adipogenesis. PMID: 12746317
22. Csk is required both for angiogenic sprouting and vascular remodeling. PMID: 14576066
23. role in regulating the permissiveness for internalization of the alphaPDGFR PMID: 14644164
24. Disruption of Ca(2+)-dependent cell matrix adhesion enhances Csk activity, but causes disssociation of the c-sarc/FAK complex and dephosphorylation of tyrosine of FAK in carcinoma cells. PMID: 14729052
25. In adult testis, however, a differential Csk immunoreactivity was found among the seminiferous tubules. PMID: 15277007
26. Csk is a critical regulator of TLR4-mediated signalling by modifying the levels of Src-like kinases. PMID: 15773898
27. Csk has a critical role in cell migration PMID: 16501257
28. Our data demonstrate that Csk is involved in the control of cGMP levels and that membrane-bound guanylyl cyclases can be critically modulated by other receptor-initiated intracellular signaling pathways. PMID: 16519534
29. Osteoclastic protein-tyrosine phosphatase (PTP-oc) activates osteoclast activity in part by promoting osteoclast survival through the PTP-oc-mediated c-Src-dependent activation of NFkappaB and JNK2. PMID: 17400176
30. Epidermal hyperplasia and hyperkeratosis in Csk-knockoutt mice were associated with an increased number of stem cells in the interfollicular epidermis and chronic inflammation in dermis and epidermal hyperplasia. PMID: 17494055
31. Whereas Ang II has an obligatory need for c-Src, ET-1 mediates its actions through a c-Src-independent Ras-Raf-dependent pathway for MAPK activation PMID: 17569879
32. In conclusion, suppression of c-Src activity stimulates muscle differentiation by activating p38 MAPK uni-directionally. PMID: 17612500
33. Src is an essential regulator of podosome structure, dynamics and organization. PMID: 17978100
34. While Gab2 co-operates with overexpressed c-Src to enhance proliferative signaling, co-expression of Gab2 with activated Src mutants promotes acinar disruption. PMID: 17998934
35. These results suggest novel roles for ZO proteins as Src/Csk scaffolds potentially involved in the regulation of Src transformation. PMID: 18086565
36. c-Src has the potential to induce cell transformation, but it requires coordination with an additional pathway(s) to promote tumor progression in vivo. PMID: 18173743
37. Inactivation of Csk caused deformities in various tissues of neural crest origins, including facial dysplasia and corneal opacity. PMID: 18262517
38. PLCgamma2 influences Src activation by mediating the localization of Src to the integrin complex and thereby regulating integrin-mediated functions in the osteoclast. PMID: 18378693
39. These findings indicate a potential role for Cbp as a suppressor of c-Src-mediated tumor progression. PMID: 18498747
40. Activation of c-Src and Fyn kinases by protein-tyrosine phosphatase RPTPalpha is substrate-specific and compatible with lipid raft localization. PMID: 18948260
41. Neutrophil transendothelial migration induced by septic alveolar macrophages is dependent on the generation of superoxide in endothelial cells via the c-Src kinase/NADPH oxidase signaling pathway. PMID: 19050294
42. The expression and activity of Src and low molecular weight protein tyrosine phosphatase (LMWPTP) during osteoblast differentiation was examined and the modulation of Src kinase by LMWPTP was assessed. PMID: 19088431
43. six genes (Csk, Itga3, Jarid2, Prkaca, Rarg, and Sall4), known to cause NTDs when deleted, that are also down-regulated in p53 -/- embryos. PMID: 19229884
44. Glucose 6-phosphate dehydrogenase is regulated through c-Src-mediated tyrosine phosphorylation in endothelial cells. PMID: 19359662
45. c-Src enhances RIG-I-mediated signaling, acting at the level of TRAF3 PMID: 19419966
46. Csk-mediated tyrosine phosphorylation is a novel molecular mechanism to limit P2X3 receptor function in mouse sensory neurons PMID: 19509283
47. that distinct SFK signaling pathways regulate mES cell fate; the formation of primitive ectoderm is regulated by the activity of c-Src PMID: 19825829
48. Anti-inflammatory role through control of the neutrophil activation threshold in vivo: suppression of premature degranulation and integrin release, neutrophil recruitment and adhesion, while supporting cell migration. PMID: 14975240

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KEGG: mmu:12988

STRING: 10090.ENSMUSP00000034863

UniGene: Mm.21974