C-Src Kinase Protein

C-Src Kinase Products

C-Src Kinase Protein, Recombinant

Molecule	Species	Description //For Detailed Info.------CLICK!	Cat No
C-Src Kinase/CSK	Human	C-Src Kinase/CSK Protein, Recombinant, with GST Tag	10740-H09B
C-Src Kinase/CSK	Mouse	CSK / C-Src kinase Protein, Recombinant, with GST Tag	50893-M20B

C-Src Kinase cDNA Clone

Molecule	Species	Description //For Detailed Info.------CLICK!	Cat No
C-Src Kinase/CSK	Human	Homo sapiens C-Src Kinase/CSK cDNA Clone	HG10740-M
C-Src Kinase/CSK	Mouse	Mouse CSK cDNA Clone / ORF Clone	MG50893-G

C-Src Kinase Related Areas

Enzyme>>Protein Kinase>>Intracellular Kinase>>C-Src Kinase/CSK

Signal Transduction>>Protein Kinase>>Intracellular Kinase>>C-Src Kinase/CSK

C-Src Kinase Alternative Names

C-Src Kinase, SRC, CSK, MGC117393, c-src tyrosine kinase [Homo sapiens]

C-Src Kinase, Src, Csk, AW212630, c-src tyrosine kinase [Mus musculus]

C-Src Kinase Background

The tyrosine kinase c-Src has been implicated as a modulator of cell proliferation, spreading, and migration. These functions are also regulated by Met. The structure of a large fragment of the c-Src kinase comprises the regulatory and kinase domains and the carboxy-terminal tall. c-Src kinase interactions among domains and is stabilized by binding of the phosphorylated tail to the SH2 domain. This molecule is locked in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase. The protein-tyrosine kinase activity of c-Src kinase is inhibited by phosphorylation of tyr527, within the c-Src c-terminal tail. Genetic and biochemical data have suggested that this negative regulation requires an intact Src homology 2 (SH2) domain. Since SH2 domains recognize phosphotyrosine, it is possible that these two non-catalytic domains associate, and thereby repress c-Src kinase activity. Experiments have suggested that c-Src kinase plays a role in the biological behaviour of colonic carcinoma cells induced by migratory factors such as EGF, perhaps acting in conjunction with FAK to regulate focal adhesion turnover and tumour cell motility. Furthermore, although c-Src kinase has been implicated in colonic tumour progression, in the adenoma to carcinoma in vitro model c-Src is not the driving force for this progression but co-operates with other molecules in carcinoma development.

References

1. Brunton VG, et al. (1997) A role for epidermal growth factor receptor, c-Src and focal adhesion kinase in an in vitro model for the progression of colon cancer. Oncogene. 14 (3): 283-93.
2. Rahimi N, et al. (1998) c-Src kinase activity is required for hepatocyte growth factor-induced motility and anchorage-independent growth of mammary carcinoma cells. J Biol Chem. 273 (50): 33714-21.
3. Liu X, et al. (1993) Regulation of c-Src tyrosine kinase activity by the Src SH2 domain. Oncogene. 8 (5): 1119-26.